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PDBsum entry 2pcb

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protein ligands Protein-protein interface(s) links
Oxidoreductase/electron transport PDB id
2pcb
Jmol
Contents
Protein chains
294 a.a. *
104 a.a. *
Ligands
HEM ×3
Waters ×337
* Residue conservation analysis
PDB id:
2pcb
Name: Oxidoreductase/electron transport
Title: Crystal structure of a complex between electron transfer partners, cytochromE C peroxidase and cytochromE C
Structure: CytochromE C peroxidase (ccp). Chain: a, c. Engineered: yes. CytochromE C. Chain: b. Engineered: yes
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Organ: heart. Equus caballus. Horse. Organism_taxid: 9796. Organ: heart
Biol. unit: Not given
Resolution:
2.80Å     R-factor:   0.178    
Authors: H.Pelletier,J.Kraut
Key ref: H.Pelletier and J.Kraut (1992). Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c. Science, 258, 1748-1755. PubMed id: 1334573 DOI: 10.1126/science.1334573
Date:
14-Apr-93     Release date:   15-Jul-93    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P00431  (CCPR_YEAST) -  Cytochrome c peroxidase, mitochondrial
Seq:
Struc:
361 a.a.
294 a.a.*
Protein chain
Pfam   ArchSchema ?
P00004  (CYC_HORSE) -  Cytochrome c
Seq:
Struc:
105 a.a.
104 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chains A, C: E.C.1.11.1.5  - Cytochrome-c peroxidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 2 ferrocytochrome c + H2O2 = 2 ferricytochrome c + 2 H2O
2 × ferrocytochrome c
+ H(2)O(2)
= 2 × ferricytochrome c
+ 2 × H(2)O
      Cofactor: Heme
Heme
Bound ligand (Het Group name = HEM) matches with 95.00% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     respiratory chain   4 terms 
  Biological process     oxidation-reduction process   4 terms 
  Biochemical function     electron carrier activity     6 terms  

 

 
    reference    
 
 
DOI no: 10.1126/science.1334573 Science 258:1748-1755 (1992)
PubMed id: 1334573  
 
 
Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c.
H.Pelletier, J.Kraut.
 
  ABSTRACT  
 
The crystal structure of a 1:1 complex between yeast cytochrome c peroxidase and yeast iso-1-cytochrome c was determined at 2.3 A resolution. This structure reveals a possible electron transfer pathway unlike any previously proposed for this extensively studied redox pair. The shortest straight line between the two hemes closely follows the peroxidase backbone chain of residues Ala194, Ala193, Gly192, and finally Trp191, the indole ring of which is perpendicular to, and in van der Waals contact with, the peroxidase heme. The crystal structure at 2.8 A of a complex between yeast cytochrome c peroxidase and horse heart cytochrome c was also determined. Although crystals of the two complexes (one with cytochrome c from yeast and the other with cytochrome c from horse) grew under very different conditions and belong to different space groups, the two complex structures are closely similar, suggesting that cytochrome c interacts with its redox partners in a highly specific manner.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21301713 C.Bernini, R.Pogni, F.J.Ruiz-Dueñas, A.T.Martínez, R.Basosi, and A.Sinicropi (2011).
EPR parameters of amino acid radicals in P. eryngii versatile peroxidase and its W164Y variant computed at the QM/MM level.
  Phys Chem Chem Phys, 13, 5078-5098.  
21359406 I.Bertini, G.Cavallaro, and A.Rosato (2011).
Principles and patterns in the interaction between mono-heme cytochrome c and its partners in electron transfer processes.
  Metallomics, 3, 354-362.  
21461416 M.Gómez-Mingot, J.Iniesta, V.Montiel, R.O.Kadara, and C.E.Banks (2011).
Screen printed graphite macroelectrodes for the direct electron transfer of cytochrome c.
  Analyst, 136, 2146-2150.  
21103575 M.H.Filby, J.Muldoon, S.Dabb, N.C.Fletcher, A.E.Ashcroft, and A.J.Wilson (2011).
Protein surface recognition using geometrically pure Ru(II) tris(bipyridine) derivatives.
  Chem Commun (Camb), 47, 559-561.  
21241885 P.H.Keizers, and M.Ubbink (2011).
Paramagnetic tagging for protein structure and dynamics analysis.
  Prog Nucl Magn Reson Spectrosc, 58, 88-96.  
21213247 P.L.Kastritis, I.H.Moal, H.Hwang, Z.Weng, P.A.Bates, A.M.Bonvin, and J.Janin (2011).
A structure-based benchmark for protein-protein binding affinity.
  Protein Sci, 20, 482-491.  
21049303 A.N.Volkov, M.Ubbink, and N.A.van Nuland (2010).
Mapping the encounter state of a transient protein complex by PRE NMR spectroscopy.
  J Biomol NMR, 48, 225-236.  
20386942 B.R.Goblirsch, B.R.Streit, J.L.Dubois, and C.M.Wilmot (2010).
Structural features promoting dioxygen production by Dechloromonas aromatica chlorite dismutase.
  J Biol Inorg Chem, 15, 879-888.
PDB codes: 3m2q 3m2s 3q08 3q09
19072042 A.M.Hays Putnam, Y.T.Lee, and D.B.Goodin (2009).
Replacement of an electron transfer pathway in cytochrome c peroxidase with a surrogate peptide.
  Biochemistry, 48, 1-3.
PDB code: 3exb
19805263 A.T.Smith, W.A.Doyle, P.Dorlet, and A.Ivancich (2009).
Spectroscopic evidence for an engineered, catalytically active Trp radical that creates the unique reactivity of lignin peroxidase.
  Proc Natl Acad Sci U S A, 106, 16084-16089.  
18987391 F.J.Ruiz-Dueñas, M.Morales, E.García, Y.Miki, M.J.Martínez, and A.T.Martínez (2009).
Substrate oxidation sites in versatile peroxidase and other basidiomycete peroxidases.
  J Exp Bot, 60, 441-452.  
19158088 F.J.Ruiz-Dueñas, R.Pogni, M.Morales, S.Giansanti, M.J.Mate, A.Romero, M.J.Martínez, R.Basosi, and A.T.Martínez (2009).
Protein radicals in fungal versatile peroxidase: catalytic tryptophan radical in both compound I and compound II and studies on W164Y, W164H, and W164S variants.
  J Biol Chem, 284, 7986-7994.
PDB code: 2w23
19522502 G.M.Clore, and J.Iwahara (2009).
Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes.
  Chem Rev, 109, 4108-4139.  
19099403 G.Saab-Rincón, and B.Valderrama (2009).
Protein engineering of redox-active enzymes.
  Antioxid Redox Signal, 11, 167-192.  
19890332 M.Nojiri, H.Koteishi, T.Nakagami, K.Kobayashi, T.Inoue, K.Yamaguchi, and S.Suzuki (2009).
Structural basis of inter-protein electron transfer for nitrite reduction in denitrification.
  Nature, 462, 117-120.
PDB code: 2zon
18231600 B.Meyer, and J.Kuever (2008).
Homology Modeling of Dissimilatory APS Reductases (AprBA) of Sulfur-Oxidizing and Sulfate-Reducing Prokaryotes.
  PLoS ONE, 3, e1514.  
17949262 I.Belevich, and M.I.Verkhovsky (2008).
Molecular mechanism of proton translocation by cytochrome C oxidase.
  Antioxid Redox Signal, 10, 1.  
19006325 J.Janzon, Q.Yuan, F.Malatesta, P.Hellwig, B.Ludwig, B.Durham, and F.Millett (2008).
Probing the Paracoccus denitrificans cytochrome c(1)-cytochrome c(552) interaction by mutagenesis and fast kinetics.
  Biochemistry, 47, 12974-12984.  
18392863 L.V.Michel, and K.L.Bren (2008).
Submolecular unfolding units of Pseudomonas aeruginosa cytochrome c-551.
  J Biol Inorg Chem, 13, 837-845.  
18389511 P.B.Crowley, P.Ganji, and H.Ibrahim (2008).
Protein surface recognition: structural characterisation of cytochrome c-porphyrin complexes.
  Chembiochem, 9, 1029-1033.  
18445553 V.Guallar, and F.Wallrapp (2008).
Mapping protein electron transfer pathways with QM/MM methods.
  J R Soc Interface, 5, S233-S239.  
18083189 Y.C.Kim, and G.Hummer (2008).
Coarse-grained models for simulations of multiprotein complexes: application to ubiquitin binding.
  J Mol Biol, 375, 1416-1433.  
18771292 Y.T.Meharenna, P.Oertel, B.Bhaskar, and T.L.Poulos (2008).
Engineering ascorbate peroxidase activity into cytochrome c peroxidase.
  Biochemistry, 47, 10324-10332.
PDB codes: 3e2n 3e2o
17205171 A.J.Wilson, J.Hong, S.Fletcher, and A.D.Hamilton (2007).
Recognition of solvent exposed protein surfaces using anthracene derived receptors.
  Org Biomol Chem, 5, 276-285.  
17275914 C.M.DiCarlo, L.B.Vitello, and J.E.Erman (2007).
Effect of active site and surface mutations on the reduction potential of yeast cytochrome c peroxidase and spectroscopic properties of the oxidized and reduced enzyme.
  J Inorg Biochem, 101, 603-613.  
17580971 N.M.Pearl, T.Jacobson, M.Arisa, L.B.Vitello, and J.E.Erman (2007).
Effect of single-site charge-reversal mutations on the catalytic properties of yeast cytochrome c peroxidase: mutations near the high-affinity cytochrome c binding site.
  Biochemistry, 46, 8263-8272.  
17001006 A.H.Talasaz, M.Nemat-Gorgani, Y.Liu, P.Ståhl, R.W.Dutton, M.Ronaghi, and R.W.Davis (2006).
Prediction of protein orientation upon immobilization on biological and nonbiological surfaces.
  Proc Natl Acad Sci U S A, 103, 14773-14778.  
17146057 A.N.Volkov, J.A.Worrall, E.Holtzmann, and M.Ubbink (2006).
Solution structure and dynamics of the complex between cytochrome c and cytochrome c peroxidase determined by paramagnetic NMR.
  Proc Natl Acad Sci U S A, 103, 18945-18950.
PDB code: 2gb8
16807958 H.A.Heering, K.A.Williams, S.de Vries, and C.Dekker (2006).
Specific vectorial immobilization of oligonucleotide-modified yeast cytochrome C on carbon nanotubes.
  Chemphyschem, 7, 1705-1709.  
16550276 H.Bayraktar, P.S.Ghosh, V.M.Rotello, and M.J.Knapp (2006).
Disruption of protein-protein interactions using nanoparticles: inhibition of cytochrome c peroxidase.
  Chem Commun (Camb), (), 1390-1392.  
16788912 J.N.Harvey, C.M.Bathelt, and A.J.Mulholland (2006).
QM/MM modeling of compound I active species in cytochrome P450, cytochrome C peroxidase, and ascorbate peroxidase.
  J Comput Chem, 27, 1352-1362.  
17098195 K.Maeda, P.Hägglund, C.Finnie, B.Svensson, and A.Henriksen (2006).
Structural basis for target protein recognition by the protein disulfide reductase thioredoxin.
  Structure, 14, 1701-1710.
PDB code: 2iwt
17128976 S.Nakani, L.B.Vitello, and J.E.Erman (2006).
Characterization of four covalently-linked yeast cytochrome c/cytochrome c peroxidase complexes: Evidence for electrostatic interaction between bound cytochrome c molecules.
  Biochemistry, 45, 14371-14378.  
16769893 T.Ueno, N.Yokoi, M.Unno, T.Matsui, Y.Tokita, M.Yamada, M.Ikeda-Saito, H.Nakajima, and Y.Watanabe (2006).
Design of metal cofactors activated by a protein-protein electron transfer system.
  Proc Natl Acad Sci U S A, 103, 9416-9421.
PDB codes: 1wzd 1wzf 1wzg
15738411 B.M.Hoffman, L.M.Celis, D.A.Cull, A.D.Patel, J.L.Seifert, K.E.Wheeler, J.Wang, J.Yao, I.V.Kurnikov, and J.M.Nocek (2005).
Differential influence of dynamic processes on forward and reverse electron transfer across a protein-protein interface.
  Proc Natl Acad Sci U S A, 102, 3564-3569.  
16234927 C.M.Bathelt, A.J.Mulholland, and J.N.Harvey (2005).
QM/MM studies of the electronic structure of the compound I intermediate in cytochrome c peroxidase and ascorbate peroxidase.
  Dalton Trans, (), 3470-3476.  
15738403 H.B.Gray, and J.R.Winkler (2005).
Long-range electron transfer.
  Proc Natl Acad Sci U S A, 102, 3534-3539.  
16151864 I.Bertini, G.Cavallaro, and A.Rosato (2005).
A structural model for the adduct between cytochrome c and cytochrome c oxidase.
  J Biol Inorg Chem, 10, 613-624.
PDB code: 1zyy
15822112 K.Mattila, and T.Haltia (2005).
How does nitrous oxide reductase interact with its electron donors?--A docking study.
  Proteins, 59, 708-722.  
16227441 S.A.Kang, and B.R.Crane (2005).
Effects of interface mutations on association modes and electron-transfer rates between proteins.
  Proc Natl Acad Sci U S A, 102, 15465-15470.
PDB codes: 2b0z 2b10 2b11 2b12
15868183 S.Hirota, H.Okumura, S.Kuroiwa, N.Funasaki, and Y.Watanabe (2005).
Reduction of ferricytochrome c by tyrosyltyrosylphenylalanine.
  J Biol Inorg Chem, 10, 355-363.  
15274917 J.M.Dias, T.Alves, C.Bonifácio, A.S.Pereira, J.Trincão, D.Bourgeois, I.Moura, and M.J.Romão (2004).
Structural basis for the mechanism of Ca(2+) activation of the di-heme cytochrome c peroxidase from Pseudomonas nautica 617.
  Structure, 12, 961-973.
PDB codes: 1nml 1rz5 1rz6
15071191 M.Guo, B.Bhaskar, H.Li, T.P.Barrows, and T.L.Poulos (2004).
Crystal structure and characterization of a cytochrome c peroxidase-cytochrome c site-specific cross-link.
  Proc Natl Acad Sci U S A, 101, 5940-5945.
PDB code: 1s6v
15386621 M.Prudêncio, and M.Ubbink (2004).
Transient complexes of redox proteins: structural and dynamic details from NMR studies.
  J Mol Recognit, 17, 524-539.  
15103624 P.B.Crowley, and M.A.Carrondo (2004).
The architecture of the binding site in redox protein complexes: implications for fast dissociation.
  Proteins, 55, 603-612.  
12538891 A.M.Hays, H.B.Gray, and D.B.Goodin (2003).
Trapping of peptide-based surrogates in an artificially created channel of cytochrome c peroxidase.
  Protein Sci, 12, 278-287.  
12567183 D.Leys, J.Basran, F.Talfournier, M.J.Sutcliffe, and N.S.Scrutton (2003).
Extensive conformational sampling in a ternary electron transfer complex.
  Nat Struct Biol, 10, 219-225.
PDB codes: 1o94 1o95 1o96 1o97
12640445 K.H.Sharp, M.Mewies, P.C.Moody, and E.L.Raven (2003).
Crystal structure of the ascorbate peroxidase-ascorbate complex.
  Nat Struct Biol, 10, 303-307.
PDB codes: 1oaf 1oag
14528294 P.Arnoux, M.Sabaty, J.Alric, B.Frangioni, B.Guigliarelli, J.M.Adriano, and D.Pignol (2003).
Structural and redox plasticity in the heterodimeric periplasmic nitrate reductase.
  Nat Struct Biol, 10, 928-934.
PDB code: 1ogy
14646081 S.Parkin, and H.Hope (2003).
Low-temperature water reconstruction in concanavalin A, with implications for controlled protein crystal annealing.
  Acta Crystallogr D Biol Crystallogr, 59, 2228-2236.  
11880631 C.Lange, and C.Hunte (2002).
Crystal structure of the yeast cytochrome bc1 complex with its bound substrate cytochrome c.
  Proc Natl Acad Sci U S A, 99, 2800-2805.
PDB code: 1kyo
11870867 D.Flöck, and V.Helms (2002).
Protein--protein docking of electron transfer complexes: cytochrome c oxidase and cytochrome c.
  Proteins, 47, 75-85.  
11842205 G.Fritz, A.Roth, A.Schiffer, T.Büchert, G.Bourenkov, H.D.Bartunik, H.Huber, K.O.Stetter, P.M.Kroneck, and U.Ermler (2002).
Structure of adenylylsulfate reductase from the hyperthermophilic Archaeoglobus fulgidus at 1.6-A resolution.
  Proc Natl Acad Sci U S A, 99, 1836-1841.
PDB codes: 1jnr 1jnz
11900539 H.Mei, L.Geren, M.A.Miller, B.Durham, and F.Millett (2002).
Role of the low-affinity binding site in electron transfer from cytochrome C to cytochrome C peroxidase.
  Biochemistry, 41, 3968-3976.  
11790838 J.Fernández-Recio, M.Totrov, and R.Abagyan (2002).
Soft protein-protein docking in internal coordinates.
  Protein Sci, 11, 280-291.  
12324399 P.Fromme, H.Bottin, N.Krauss, and P.Sétif (2002).
Crystallization and electron paramagnetic resonance characterization of the complex of photosystem I with its natural electron acceptor ferredoxin.
  Biophys J, 83, 1760-1773.  
11967381 R.J.Rosenfeld, A.M.Hays, R.A.Musah, and D.B.Goodin (2002).
Excision of a proposed electron transfer pathway in cytochrome c peroxidase and its replacement by a ligand-binding channel.
  Protein Sci, 11, 1251-1259.
PDB codes: 1kxm 1kxn
12411478 V.A.Bamford, S.Bruno, T.Rasmussen, C.Appia-Ayme, M.R.Cheesman, B.C.Berks, and A.M.Hemmings (2002).
Structural basis for the oxidation of thiosulfate by a sulfur cycle enzyme.
  EMBO J, 21, 5599-5610.
PDB codes: 1h31 1h32 1h33
11159430 A.H.Elcock, and J.A.McCammon (2001).
Calculation of weak protein-protein interactions: the pH dependence of the second virial coefficient.
  Biophys J, 80, 613-625.  
11141081 A.S.Morar, X.Wang, and G.J.Pielak (2001).
Effects of crowding by mono-, di-, and tetrasaccharides on cytochrome c-cytochrome c peroxidase binding: comparing experiment to theory.
  Biochemistry, 40, 281-285.  
11296248 F.A.Tezcan, B.R.Crane, J.R.Winkler, and H.B.Gray (2001).
Electron tunneling in protein crystals.
  Proc Natl Acad Sci U S A, 98, 5002-5006.
PDB codes: 1i54 1i55
11396482 G.Battistuzzi, M.Borsari, and M.Sola (2001).
Redox properties of cytochrome c.
  Antioxid Redox Signal, 3, 279-291.  
11148036 G.J.Pielak, and X.Wang (2001).
Interactions between yeast iso-1-cytochrome c and its peroxidase.
  Biochemistry, 40, 422-428.  
11170452 J.Hirst, S.K.Wilcox, P.A.Williams, J.Blankenship, D.E.McRee, and D.B.Goodin (2001).
Replacement of the axial histidine ligand with imidazole in cytochrome c peroxidase. 1. Effects on structure.
  Biochemistry, 40, 1265-1273.
PDB codes: 1ds4 1dse 1dsg 1dso 1dsp
11133964 M.Santana, M.M.Pereira, N.P.Elias, C.M.Soares, and M.Teixeira (2001).
Gene cluster of Rhodothermus marinus high-potential iron-sulfur Protein: oxygen oxidoreductase, a caa(3)-type oxidase belonging to the superfamily of heme-copper oxidases.
  J Bacteriol, 183, 687-699.  
11502207 P.D.Barker, I.Bertini, R.Del Conte, S.J.Ferguson, P.Hajieva, E.Tomlinson, P.Turano, and M.S.Viezzoli (2001).
A further clue to understanding the mobility of mitochondrial yeast cytochrome c: a (15)N T1rho investigation of the oxidized and reduced species.
  Eur J Biochem, 268, 4468-4476.  
11893069 S.Hirota, and O.Yamauchi (2001).
Weak interactions and molecular recognition in systems involving electron transfer proteins.
  Chem Rec, 1, 290-299.  
11567104 X.J.Morelli, P.N.Palma, F.Guerlesquin, and A.C.Rigby (2001).
A novel approach for assessing macromolecular complexes combining soft-docking calculations with NMR data.
  Protein Sci, 10, 2131-2137.  
11268087 Y.Hitomi, T.Hayashi, K.Wada, T.Mizutani, Y.Hisaeda, and H.Ogoshi (2001).
Interprotein Electron Transfer Reaction Regulated by an Artificial Interface We thank Prof. Dr. I. Morishima and his group for the arrangement of laser flash photolysis equipment. This work was supported by Nagase Science and Technology Foundation, and a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture, Japan. Y. H. was supported by Research Fellowships of the Japanese Society for the Promotion of Science for Young Scientists.
  Angew Chem Int Ed Engl, 40, 1098-1101.  
10978164 A.Iffland, P.Tafelmeyer, C.Saudan, and K.Johnsson (2000).
Directed molecular evolution of cytochrome c peroxidase.
  Biochemistry, 39, 10790-10798.  
10866825 P.Pristovsek, C.Lücke, B.Reincke, B.Ludwig, and H.Rüterjans (2000).
Solution structure of the functional domain of Paracoccus denitrificans cytochrome c552 in the reduced state.
  Eur J Biochem, 267, 4205-4212.
PDB code: 1c7m
11053838 R.Morales, G.Kachalova, F.Vellieux, M.H.Charon, and M.Frey (2000).
Crystallographic studies of the interaction between the ferredoxin-NADP+ reductase and ferredoxin from the cyanobacterium Anabaena: looking for the elusive ferredoxin molecule.
  Acta Crystallogr D Biol Crystallogr, 56, 1408-1412.
PDB code: 1ewy
11256611 R.Morales, M.H.Charon, G.Kachalova, L.Serre, M.Medina, C.Gómez-Moreno, and M.Frey (2000).
A redox-dependent interaction between two electron-transfer partners involved in photosynthesis.
  EMBO Rep, 1, 271-276.  
10771429 V.R.Samygina, S.V.Antonyuk, V.S.Lamzin, and A.N.Popov (2000).
Improving the X-ray resolution by reversible flash-cooling combined with concentration screening, as exemplified with PPase.
  Acta Crystallogr D Biol Crystallogr, 56, 595-603.  
10956001 V.W.Leesch, J.Bujons, A.G.Mauk, and B.M.Hoffman (2000).
Cytochrome c peroxidase-cytochrome c complex: locating the second binding domain on cytochrome c peroxidase with site-directed mutagenesis.
  Biochemistry, 39, 10132-10139.  
10625444 A.Osyczka, K.V.Nagashima, S.Sogabe, K.Miki, K.Shimada, and K.Matsuura (1999).
Comparison of the binding sites for high-potential iron-sulfur protein and cytochrome c on the tetraheme cytochrome subunit bound to the bacterial photosynthetic reaction center.
  Biochemistry, 38, 15779-15790.  
10220341 C.A.Bonagura, M.Sundaramoorthy, B.Bhaskar, and T.L.Poulos (1999).
The effects of an engineered cation site on the structure, activity, and EPR properties of cytochrome c peroxidase.
  Biochemistry, 38, 5538-5545.
PDB code: 1jdr
9987124 F.J.Ruiz-Dueñas, M.J.Martínez, and A.T.Martínez (1999).
Molecular characterization of a novel peroxidase isolated from the ligninolytic fungus Pleurotus eryngii.
  Mol Microbiol, 31, 223-235.
PDB code: 1a20
10346906 H.Mei, K.Wang, N.Peffer, G.Weatherly, D.S.Cohen, M.Miller, G.Pielak, B.Durham, and F.Millett (1999).
Role of configurational gating in intracomplex electron transfer from cytochrome c to the radical cation in cytochrome c peroxidase.
  Biochemistry, 38, 6846-6854.  
10226044 I.Bertini, and C.Luchinat (1999).
New applications of paramagnetic NMR in chemical biology.
  Curr Opin Chem Biol, 3, 145-151.  
10194370 J.S.Fetrow, and S.M.Baxter (1999).
Assignment of 15N chemical shifts and 15N relaxation measurements for oxidized and reduced iso-1-cytochrome c.
  Biochemistry, 38, 4480-4492.  
10606521 X.Wang, and G.J.Pielak (1999).
Equilibrium thermodynamics of a physiologically-relevant heme-protein complex.
  Biochemistry, 38, 16876-16881.  
9485359 C.Aubert, M.T.Giudici-Orticoni, M.Czjzek, R.Haser, M.Bruschi, and A.Dolla (1998).
Structural and kinetic studies of the Y73E mutant of octaheme cytochrome c3 (Mr = 26 000) from Desulfovibrio desulfuricans Norway.
  Biochemistry, 37, 2120-2130.
PDB code: 1aqe
9860877 D.Mandelman, J.Jamal, and T.L.Poulos (1998).
Identification of two electron-transfer sites in ascorbate peroxidase using chemical modification, enzyme kinetics, and crystallography.
  Biochemistry, 37, 17610-17617.  
9790675 G.M.Soriano, M.V.Ponamarev, R.A.Piskorowski, and W.A.Cramer (1998).
Identification of the basic residues of cytochrome f responsible for electrostatic docking interactions with plastocyanin in vitro: relevance to the electron transfer reaction in vivo.
  Biochemistry, 37, 15120-15128.  
9649404 J.A.Kornblatt, M.J.Kornblatt, I.Rajotte, G.H.Hoa, and P.C.Kahn (1998).
Thermodynamic volume cycles for electron transfer in the cytochrome c oxidase and for the binding of cytochrome c to cytochrome c oxidase.
  Biophys J, 75, 435-444.  
9485396 J.S.Fetrow, J.S.Spitzer, B.M.Gilden, S.J.Mellender, T.J.Begley, B.J.Haas, and T.L.Boose (1998).
Structure, function, and temperature sensitivity of directed, random mutants at proline 76 and glycine 77 in omega-loop D of yeast iso-1-cytochrome c.
  Biochemistry, 37, 2477-2487.  
10036970 Q.Lin, H.S.Park, Y.Hamuro, C.S.Lee, and A.D.Hamilton (1998).
Protein surface recognition by synthetic agents: design and structural requirements of a family of artificial receptors that bind to cytochrome c.
  Biopolymers, 47, 285-297.  
  9514261 Y.Cao, R.A.Musah, S.K.Wilcox, D.B.Goodin, and D.E.McRee (1998).
Protein conformer selection by ligand binding observed with crystallography.
  Protein Sci, 7, 72-78.
PDB code: 1ccj
9346287 A.P.Hill, S.Modi, M.J.Sutcliffe, D.D.Turner, D.J.Gilfoyle, A.T.Smith, B.M.Tam, and E.Lloyd (1997).
Chemical, spectroscopic and structural investigation of the substrate-binding site in ascorbate peroxidase.
  Eur J Biochem, 248, 347-354.  
  9416602 D.M.Hoover, and M.L.Ludwig (1997).
A flavodoxin that is required for enzyme activation: the structure of oxidized flavodoxin from Escherichia coli at 1.8 A resolution.
  Protein Sci, 6, 2525-2537.
PDB codes: 1ag9 1ahn
9048579 E.Monzani, A.L.Gatti, A.Profumo, L.Casella, and M.Gullotti (1997).
Oxidation of phenolic compounds by lactoperoxidase. Evidence for the presence of a low-potential compound II during catalytic turnover.
  Biochemistry, 36, 1918-1926.  
8993335 H.Wendt, L.Leder, H.Härmä, I.Jelesarov, A.Baici, and H.R.Bosshard (1997).
Very rapid, ionic strength-dependent association and folding of a heterodimeric leucine zipper.
  Biochemistry, 36, 204-213.  
9092837 J.E.Erman, G.C.Kresheck, L.B.Vitello, and M.A.Miller (1997).
Cytochrome c/cytochrome c peroxidase complex: effect of binding-site mutations on the thermodynamics of complex formation.
  Biochemistry, 36, 4054-4060.  
  9007992 J.S.Fetrow, S.R.Horner, W.Oehrl, D.L.Schaak, T.L.Boose, and R.E.Burton (1997).
Analysis of the structure and stability of omega loop A replacements in yeast iso-1-cytochrome c.
  Protein Sci, 6, 197-210.  
9245419 L.Banci, I.Bertini, H.B.Gray, C.Luchinat, T.Reddig, A.Rosato, and P.Turano (1997).
Solution structure of oxidized horse heart cytochrome c.
  Biochemistry, 36, 9867-9877.
PDB code: 1akk
9220987 L.Banci, I.Bertini, K.L.Bren, H.B.Gray, P.Sompornpisut, and P.Turano (1997).
Solution structure of oxidized Saccharomyces cerevisiae iso-1-cytochrome c.
  Biochemistry, 36, 8992-9001.
PDB code: 1yic
  9278152 L.Piubelli, G.Zanetti, and H.R.Bosshard (1997).
Recombinant wild-type and mutant complexes of ferredoxin and ferredoxin:NADP+ reductase studied by isothermal titration calorimetry.
  Biol Chem, 378, 715-718.  
9174347 M.Ubbink, and D.S.Bendall (1997).
Complex of plastocyanin and cytochrome c characterized by NMR chemical shift analysis.
  Biochemistry, 36, 6326-6335.  
9245408 R.E.Whitwam, K.R.Brown, M.Musick, M.J.Natan, and M.Tien (1997).
Mutagenesis of the Mn2+-binding site of manganese peroxidase affects oxidation of Mn2+ by both compound I and compound II.
  Biochemistry, 36, 9766-9773.  
9136887 S.F.Sukits, J.E.Erman, and J.D.Satterlee (1997).
Proton NMR assignments and magnetic axes orientations for wild-type yeast iso-1-ferricytochrome c free in solution and bound to cytochrome c peroxidase.
  Biochemistry, 36, 5251-5259.  
9335529 V.L.Davidson, L.H.Jones, M.E.Graichen, F.S.Mathews, and J.P.Hosler (1997).
Factors which stabilize the methylamine dehydrogenase-amicyanin electron transfer protein complex revealed by site-directed mutagenesis.
  Biochemistry, 36, 12733-12738.  
9335558 W.N.Lanzilotta, and L.C.Seefeldt (1997).
Changes in the midpoint potentials of the nitrogenase metal centers as a result of iron protein-molybdenum-iron protein complex formation.
  Biochemistry, 36, 12976-12983.  
9354631 Y.Feng, and R.P.Swenson (1997).
Evaluation of the role of specific acidic amino acid residues in electron transfer between the flavodoxin and cytochrome c3 from Desulfovibrio vulgaris.
  Biochemistry, 36, 13617-13628.  
9283079 Z.H.Zhou, and M.W.Adams (1997).
Site-directed mutations of the 4Fe-ferredoxin from the hyperthermophilic archaeon Pyrococcus furiosus: role of the cluster-coordinating aspartate in physiological electron transfer reactions.
  Biochemistry, 36, 10892-10900.  
8634253 C.A.Bonagura, M.Sundaramoorthy, H.S.Pappa, W.R.Patterson, and T.L.Poulos (1996).
An engineered cation site in cytochrome c peroxidase alters the reactivity of the redox active tryptophan.
  Biochemistry, 35, 6107-6115.  
8805539 D.J.Schuller, N.Ban, R.B.Huystee, A.McPherson, and T.L.Poulos (1996).
The crystal structure of peanut peroxidase.
  Structure, 4, 311-321.
PDB code: 1sch
8931557 G.M.Soriano, M.V.Ponamarev, G.S.Tae, and W.A.Cramer (1996).
Effect of the interdomain basic region of cytochrome f on its redox reactions in vivo.
  Biochemistry, 35, 14590-14598.  
8961943 H.Mei, K.Wang, S.McKee, X.Wang, J.L.Waldner, G.J.Pielak, B.Durham, and F.Millett (1996).
Control of formation and dissociation of the high-affinity complex between cytochrome c and cytochrome c peroxidase by ionic strength and the low-affinity binding site.
  Biochemistry, 35, 15800-15806.  
8664274 H.S.Pappa, S.Tajbaksh, A.J.Saunders, G.J.Pielak, and T.L.Poulos (1996).
Probing the cytochrome c peroxidase-cytochrome c electron transfer reaction using site specific cross-linking.
  Biochemistry, 35, 4837-4845.  
8555215 J.Wang, R.W.Larsen, S.J.Moench, J.D.Satterlee, D.L.Rousseau, and M.R.Ondrias (1996).
Cytochrome c peroxidase complexed with cytochrome c has an unperturbed heme moiety.
  Biochemistry, 35, 453-463.  
8942678 K.Wang, H.Mei, L.Geren, M.A.Miller, A.Saunders, X.Wang, J.L.Waldner, G.J.Pielak, B.Durham, and F.Millett (1996).
Design of a ruthenium-cytochrome c derivative to measure electron transfer to the radical cation and oxyferryl heme in cytochrome c peroxidase.
  Biochemistry, 35, 15107-15119.  
8639487 L.Qin, and N.M.Kostić (1996).
Enforced interaction of one molecule of plastocyanin with two molecules of cytochrome c and an electron-transfer reaction involving the hydrophobic patch on the plastocyanin surface.
  Biochemistry, 35, 3379-3386.  
8547245 M.A.Miller, L.Geren, G.W.Han, A.Saunders, J.Beasley, G.J.Pielak, B.Durham, F.Millett, and J.Kraut (1996).
Identifying the physiological electron transfer site of cytochrome c peroxidase by structure-based engineering.
  Biochemistry, 35, 667-673.
PDB code: 1cyf
8961942 M.A.Miller (1996).
A complete mechanism for steady-state oxidation of yeast cytochrome c by yeast cytochrome c peroxidase.
  Biochemistry, 35, 15791-15799.  
8740362 M.Czjzek, F.Guerlesquin, M.Bruschi, and R.Haser (1996).
Crystal structure of a dimeric octaheme cytochrome c3 (M(r) 26,000) from Desulfovibrio desulfuricans Norway.
  Structure, 4, 395-404.
PDB code: 1czj
8987979 M.M.Crnogorac, C.Shen, S.Young, O.Hansson, and N.M.Kostić (1996).
Effects of mutations in plastocyanin on the kinetics of the protein rearrangement gating the electron-transfer reaction with zinc cytochrome c. Analysis of the rearrangement pathway.
  Biochemistry, 35, 16465-16474.  
8942677 M.M.Ivković-Jensen, and N.M.Kostić (1996).
Effects of temperature on the kinetics of the gated electron-transfer reaction between zinc cytochrome c and plastocyanin. Analysis of configurational fluctuation of the diprotein complex.
  Biochemistry, 35, 15095-15106.  
8611557 N.Adir, H.L.Axelrod, P.Beroza, R.A.Isaacson, S.H.Rongey, M.Y.Okamura, and G.Feher (1996).
Co-crystallization and characterization of the photosynthetic reaction center-cytochrome c2 complex from Rhodobacter sphaeroides.
  Biochemistry, 35, 2535-2547.  
8901521 P.Baistrocchi, L.Banci, I.Bertini, P.Turano, K.L.Bren, and H.B.Gray (1996).
Three-dimensional solution structure of Saccharomyces cerevisiae reduced iso-1-cytochrome c.
  Biochemistry, 35, 13788-13796.
PDB code: 1yfc
8823161 P.X.Qi, R.A.Beckman, and A.J.Wand (1996).
Solution structure of horse heart ferricytochrome c and detection of redox-related structural changes by high-resolution 1H NMR.
  Biochemistry, 35, 12275-12286.
PDB codes: 1ocd 2frc
8599759 R.D.Guiles, S.Sarma, R.J.DiGate, D.Banville, V.J.Basus, I.D.Kuntz, and L.Waskell (1996).
Pseudocontact shifts used in the restraint of the solution structures of electron transfer complexes.
  Nat Struct Biol, 3, 333-339.  
8942679 R.Sinclair, S.Hallam, M.Chen, B.Chance, and L.Powers (1996).
Active site structure in cytochrome c peroxidase and myoglobin mutants: effects of altered hydrogen bonding to the proximal histidine.
  Biochemistry, 35, 15120-15128.  
8664277 S.K.Wilcox, G.M.Jensen, M.M.Fitzgerald, D.E.McRee, and D.B.Goodin (1996).
Altering substrate specificity at the heme edge of cytochrome c peroxidase.
  Biochemistry, 35, 4858-4866.
PDB codes: 3ccx 4ccx
9010601 T.C.Pochapsky, T.A.Lyons, S.Kazanis, T.Arakaki, and G.Ratnaswamy (1996).
A structure-based model for cytochrome P450cam-putidaredoxin interactions.
  Biochimie, 78, 723-733.  
8679563 V.L.Davidson, and L.H.Jones (1996).
Electron transfer from copper to heme within the methylamine dehydrogenase--amicyanin--cytochrome c-551i complex.
  Biochemistry, 35, 8120-8125.  
8847345 A.G.Mauk, M.R.Mauk, G.R.Moore, and S.H.Northrup (1995).
Experimental and theoretical analysis of the interaction between cytochrome c and cytochrome b5.
  J Bioenerg Biomembr, 27, 311-330.  
7746145 B.Heym, P.M.Alzari, N.Honoré, and S.T.Cole (1995).
Missense mutations in the catalase-peroxidase gene, katG, are associated with isoniazid resistance in Mycobacterium tuberculosis.
  Mol Microbiol, 15, 235-245.  
8847340 C.C.Moser, C.C.Page, R.Farid, and P.L.Dutton (1995).
Biological electron transfer.
  J Bioenerg Biomembr, 27, 263-274.  
8847347 F.Millett, M.A.Miller, L.Geren, and B.Durham (1995).
Electron transfer between cytochrome c and cytochrome c peroxidase.
  J Bioenerg Biomembr, 27, 341-351.  
  8665467 J.M.Musser (1995).
Antimicrobial agent resistance in mycobacteria: molecular genetic insights.
  Clin Microbiol Rev, 8, 496-514.  
  7628463 L.S.Conrad, J.J.Karlsson, and J.Ulstrup (1995).
Electron transfer and spectral alpha-band properties of the di-heme protein cytochrome c4 from Pseudomonas stutzeri.
  Eur J Biochem, 231, 133-141.  
7588806 M.T.Bes, A.L.De Lacey, M.L.Peleato, V.M.Fernandez, and C.Gómez-Moreno (1995).
The covalent linkage of a viologen to a flavoprotein reductase transforms it into an oxidase.
  Eur J Biochem, 233, 593-599.  
7583671 P.A.Williams, V.Fülöp, Y.C.Leung, C.Chan, J.W.Moir, G.Howlett, S.J.Ferguson, S.E.Radford, and J.Hajdu (1995).
Pseudospecific docking surfaces on electron transfer proteins as illustrated by pseudoazurin, cytochrome c550 and cytochrome cd1 nitrite reductase.
  Nat Struct Biol, 2, 975-982.
PDB code: 1adw
8591047 R.Sanishvili, K.W.Volz, E.M.Westbrook, and E.Margoliash (1995).
The low ionic strength crystal structure of horse cytochrome c at 2.1 A resolution and comparison with its high ionic strength counterpart.
  Structure, 3, 707-716.
PDB code: 1crc
  7757009 T.P.Lo, M.E.Murphy, J.G.Guillemette, M.Smith, and G.D.Brayer (1995).
Replacements in a conserved leucine cluster in the hydrophobic heme pocket of cytochrome c.
  Protein Sci, 4, 198-208.
PDB codes: 1csu 1csv 1csw 1csx
8591033 V.Fülöp, C.J.Ridout, C.Greenwood, and J.Hajdu (1995).
Crystal structure of the di-haem cytochrome c peroxidase from Pseudomonas aeruginosa.
  Structure, 3, 1225-1233.
PDB code: 1eb7
7736589 V.Fülöp, J.W.Moir, S.J.Ferguson, and J.Hajdu (1995).
The anatomy of a bifunctional enzyme: structural basis for reduction of oxygen to water and synthesis of nitric oxide by cytochrome cd1.
  Cell, 81, 369-377.
PDB code: 1qks
8847342 W.B.Curry, M.D.Grabe, I.V.Kurnikov, S.S.Skourtis, D.N.Beratan, J.J.Regan, A.J.Aquino, P.Beroza, and J.N.Onuchic (1995).
Pathways, pathway tubes, pathway docking, and propagators in electron transfer proteins.
  J Bioenerg Biomembr, 27, 285-293.  
  7703857 J.A.Watkins, M.A.Cusanovich, T.E.Meyer, and G.Tollin (1994).
A "parallel plate" electrostatic model for bimolecular rate constants applied to electron transfer proteins.
  Protein Sci, 3, 2104-2114.  
7511810 J.Cherfils, T.Bizebard, M.Knossow, and J.Janin (1994).
Rigid-body docking with mutant constraints of influenza hemagglutinin with antibody HC19.
  Proteins, 18, 8.  
8076654 J.D.Satterlee, S.L.Alam, J.M.Mauro, J.E.Erman, and T.L.Poulos (1994).
The effect of the Asn82-->Asp mutation in yeast cytochrome c peroxidase studied by proton NMR spectroscopy.
  Eur J Biochem, 224, 81-87.  
7972020 M.A.Miller, G.W.Han, and J.Kraut (1994).
A cation binding motif stabilizes the compound I radical of cytochrome c peroxidase.
  Proc Natl Acad Sci U S A, 91, 11118-11122.
PDB codes: 1cpd 1cpe 1cpf 1cpg
7656052 M.F.Jeng, S.W.Englander, K.Pardue, J.S.Rogalskyj, and G.McLendon (1994).
Structural dynamics in an electron-transfer complex.
  Nat Struct Biol, 1, 234-238.  
8020493 M.Ubbink, N.I.Hunt, H.A.Hill, and G.W.Canters (1994).
Kinetics of the reduction of wild-type and mutant cytochrome c-550 by methylamine dehydrogenase and amicyanin from Thiobacillus versutus.
  Eur J Biochem, 222, 561-571.  
8081747 S.E.Martinez, D.Huang, A.Szczepaniak, W.A.Cramer, and J.L.Smith (1994).
Crystal structure of chloroplast cytochrome f reveals a novel cytochrome fold and unexpected heme ligation.
  Structure, 2, 95.
PDB code: 1ctm
8081757 T.B.Karpishin, M.W.Grinstaff, S.Komar-Panicucci, G.McLendon, and H.B.Gray (1994).
Electron transfer in cytochrome c depends upon the structure of the intervening medium.
  Structure, 2, 415-422.  
8069633 V.Fülöp, R.P.Phizackerley, S.M.Soltis, I.J.Clifton, S.Wakatsuki, J.Erman, J.Hajdu, and S.L.Edwards (1994).
Laue diffraction study on the structure of cytochrome c peroxidase compound I.
  Structure, 2, 201-208.
PDB code: 1ebe
  8102922 A.R.De Pascalis, I.Jelesarov, F.Ackermann, W.H.Koppenol, M.Hirasawa, D.B.Knaff, and H.R.Bosshard (1993).
Binding of ferredoxin to ferredoxin:NADP+ oxidoreductase: the role of carboxyl groups, electrostatic surface potential, and molecular dipole moment.
  Protein Sci, 2, 1126-1135.  
8218918 H.X.Zhou (1993).
Boundary element solution of macromolecular electrostatics: interaction energy between two proteins.
  Biophys J, 65, 955-963.  
8241386 J.A.Kornblatt, M.J.Kornblatt, G.H.Hoa, and A.G.Mauk (1993).
Responses of two protein-protein complexes to solvent stress: does water play a role at the interface?
  Biophys J, 65, 1059-1065.  
8395046 M.Tegoni, S.A.White, A.Roussel, F.S.Mathews, and C.Cambillau (1993).
A hypothetical complex between crystalline flavocytochrome b2 and cytochrome c.
  Proteins, 16, 408-422.  
7764068 T.L.Poulos (1993).
Peroxidases.
  Curr Opin Biotechnol, 4, 484-489.  
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