spacer
spacer

PDBsum entry 1fcb
Go to PDB code: 
protein ligands Protein-protein interface(s) links
Oxidoreductase (ch-oh(d)-cytochrome(a)) PDB id
1fcb

 

 

 

 

Loading ...

 
JSmol PyMol  
Contents
Protein chains
494 a.a. *
400 a.a. *
Ligands
HEM
FMN ×2
PYR
Waters ×283
* Residue conservation analysis
PDB id:
1fcb
Name: Oxidoreductase (ch-oh(d)-cytochrome(a))
Title: Molecular structure of flavocytochrome b2 at 2.4 angstroms resolution
Structure: Flavocytochrome b2. Chain: a, b. Engineered: yes
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932
Biol. unit: Tetramer (from PQS)
Resolution:
2.40Å     R-factor:   0.188    
Authors: F.S.Mathews,Z.-X.Xia
Key ref: Z.X.Xia and F.S.Mathews (1990). Molecular structure of flavocytochrome b2 at 2.4 A resolution. J Mol Biol, 212, 837-863. PubMed id: 2329585
Date:
16-Jan-90     Release date:   15-Jan-91    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00175  (CYB2_YEAST) -  L-lactate dehydrogenase (cytochrome) from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc: 		 
Seq:
Struc: 		591 a.a.
494 a.a.
Protein chain
Pfam   ArchSchema ?
P00175  (CYB2_YEAST) -  L-lactate dehydrogenase (cytochrome) from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc: 		 
Seq:
Struc: 		591 a.a.
400 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B: E.C.1.1.2.3  - L-lactate dehydrogenase (cytochrome).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: (S)-lactate + 2 Fe(III)-[cytochrome c] = 2 Fe(II)-[cytochrome c] + pyruvate + 2 H+
(S)-lactate
Bound ligand (Het Group name = PYR)
corresponds exactly 		+ 2 × Fe(III)-[cytochrome c]
 = 2 × Fe(II)-[cytochrome c]
 + pyruvate
 + 2 × H(+)
      Cofactor: FMN; Heme b
FMN
Bound ligand (Het Group name = FMN) corresponds exactly
Heme b
Bound ligand (Het Group name = HEM) matches with 95.45% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
J Mol Biol 212:837-863 (1990)
PubMed id: 2329585  
 
 
Molecular structure of flavocytochrome b2 at 2.4 A resolution.
Z.X.Xia, F.S.Mathews.
 
  ABSTRACT  
 
The crystal structure of flavocytochrome b2 has been solved at 3.0 A resolution by the method of multiple isomorphous replacement with anomalous scattering. Area detector data from native and two heavy-atom derivative crystals were used. The phases were refined by the B.C. Wang phase-filtering procedure utilizing the 67% (v/v) solvent content of the crystals. A molecular model was built first on a minimap and then on computer graphics from a combination of maps both averaged and not averaged about the molecular symmetry axis. The structure was extended to 2.4 A resolution using film data recorded at a synchrotron and refined by the Hendrickson-Konnert procedure. The molecule, a tetramer of Mr 230,000, is located on a crystallographic 2-fold axis and possesses local 4-fold symmetry. Each subunit is composed of two domains, one binding a heme and the other an FMN prosthetic group. In subunit 1, both the cystochrome and the flavin-binding domain are visible in the electron density map. In subunit 2 the cytochrome domain is disordered. However, in the latter, a molecule of pyruvate, the product of the enzymatic reaction, is bound at the active site. The cytochrome domain consists of residues 1 to 99 and is folded in a fashion similar to the homologous soluble fragment of cytochrome b5. The flavin binding domain contains a parallel beta 8 alpha 8 barrel structure and is composed of residues 100 to 486. The remaining 25 residues form a tail that wraps around the molecular 4-fold axis and is in contact with each remaining subunit. The FMN moiety, which is located at the C-terminal end of the central beta-barrel, is mostly sequestered from solvent; it forms hydrogen bond interactions with main- and side-chain atoms from six of the eight beta-strands. The interaction of Lys349 with atoms N-1 and O-2 of the flavin ring is probably responsible for stabilization of the anionic form of the flavin semiquinone and hydroquinone and enhancing the reactivity of atom N-5 toward sulfite. The binding of pyruvate at the active site in subunit 2 is stabilized by interaction of its carboxylate group with the side-chain atoms of Arg376 and Tyr143. Residues His373 and Tyr254 interact with the keto-oxygen atom and are involved in catalysis. In contrast, four water molecules occupy the substrate-binding site in subunit 1 and Tyr143 forms a hydrogen bond to the ordered heme propionate group. Otherwise the two flavin-binding domains are identical within experimental error.(ABSTRACT TRUNCATED AT 400 WORDS)
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20074210 L.Lindqvist, S.Apostol, C.El Hanine-Lmoumene, and F.Lederer (2010).
Dynamics of flavin semiquinone protolysis in L-alpha-hydroxyacid-oxidizing flavoenzymes--a study using nanosecond laser flash photolysis.
  FEBS J, 277, 964-972.  
19348008 G.Tabacchi, D.Zucchini, G.Caprini, A.Gamba, F.Lederer, M.A.Vanoni, and E.Fois (2009).
L-lactate dehydrogenation in flavocytochrome b2: a first principles molecular dynamics study.
  FEBS J, 276, 2368-2380.  
19465768 N.Sukumar, A.Dewanti, A.Merli, G.L.Rossi, B.Mitra, and F.S.Mathews (2009).
Structures of the G81A mutant form of the active chimera of (S)-mandelate dehydrogenase and its complex with two of its substrates.
  Acta Crystallogr D Biol Crystallogr, 65, 543-552.
PDB codes: 2a7n 2a7p 2a85 3giy
18215067 M.S.Murray, R.P.Holmes, and W.T.Lowther (2008).
Active site and loop 4 movements within human glycolate oxidase: implications for substrate specificity and drug design.
  Biochemistry, 47, 2439-2449.
PDB codes: 2rdt 2rdu 2rdw
17563122 C.L.Tsai, K.Gokulan, P.Sobrado, J.C.Sacchettini, and P.F.Fitzpatrick (2007).
Mechanistic and structural studies of H373Q flavocytochrome b2: effects of mutating the active site base.
  Biochemistry, 46, 7844-7851.
PDB code: 2oz0
17506039 G.Tabacchi, M.A.Vanoni, A.Gamba, and E.Fois (2007).
Does negative hyperconjugation assist enzymatic dehydrogenations?
  Chemphyschem, 8, 1283-1288.  
17074805 M.Krayl, J.H.Lim, F.Martin, B.Guiard, and W.Voos (2007).
A cooperative action of the ATP-dependent import motor complex and the inner membrane potential drives mitochondrial preprotein import.
  Mol Cell Biol, 27, 411-425.  
  19890477 P.F.Fitzpatrick (2007).
Insights into the mechanisms of flavoprotein oxidases from kinetic isotope effects.
  J Labelled Comp Radiopharm, 50, 1016-1025.  
16600599 A.Mattevi (2006).
To be or not to be an oxidase: challenging the oxygen reactivity of flavoenzymes.
  Trends Biochem Sci, 31, 276-283.  
16407065 D.C.Lamb, Y.Kim, L.V.Yermalitskaya, V.N.Yermalitsky, G.I.Lepesheva, S.L.Kelly, M.R.Waterman, and L.M.Podust (2006).
A second FMN binding site in yeast NADPH-cytochrome P450 reductase suggests a mechanism of electron transfer by diflavin reductases.
  Structure, 14, 51-61.
PDB codes: 2bf4 2bn4
17046020 I.M.Moustafa, S.Foster, A.Y.Lyubimov, and A.Vrielink (2006).
Crystal structure of LAAO from Calloselasma rhodostoma with an L-phenylalanine substrate: insights into structure and mechanism.
  J Mol Biol, 364, 991.
PDB code: 2iid
16040738 A.I.Ioanitescu, S.Dewilde, L.Kiger, M.C.Marden, L.Moens, and S.Van Doorslaer (2005).
Characterization of nonsymbiotic tomato hemoglobin.
  Biophys J, 89, 2628-2639.  
16336126 B.von Janowsky, K.Knapp, T.Major, M.Krayl, B.Guiard, and W.Voos (2005).
Structural properties of substrate proteins determine their proteolysis by the mitochondrial AAA+ protease Pim1.
  Biol Chem, 386, 1307-1317.  
16204505 C.Stansen, D.Uy, S.Delaunay, L.Eggeling, J.L.Goergen, and V.F.Wendisch (2005).
Characterization of a Corynebacterium glutamicum lactate utilization operon induced during temperature-triggered glutamate production.
  Appl Environ Microbiol, 71, 5920-5928.  
16314970 H.Kaneko, H.Minagawa, and J.Shimada (2005).
Rational design of thermostable lactate oxidase by analyzing quaternary structure and prevention of deamidation.
  Biotechnol Lett, 27, 1777-1784.  
  16511063 Y.Umena, K.Yorita, T.Matsuoka, M.Abe, A.Kita, K.Fukui, T.Tsukihara, and Y.Morimoto (2005).
Crystallization and preliminary X-ray diffraction study of L-lactate oxidase (LOX), R181M mutant, from Aerococcus viridans.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 61, 439-441.  
14604988 N.Sukumar, A.R.Dewanti, B.Mitra, and F.S.Mathews (2004).
High resolution structures of an oxidized and reduced flavoprotein. The water switch in a soluble form of (S)-mandelate dehydrogenase.
  J Biol Chem, 279, 3749-3757.
PDB codes: 1p4c 1p5b
15375150 P.Goffin, F.Lorquet, M.Kleerebezem, and P.Hols (2004).
Major role of NAD-dependent lactate dehydrogenases in aerobic lactate utilization in Lactobacillus plantarum during early stationary phase.
  J Bacteriol, 186, 6661-6666.  
15502298 S.Bando, T.Takano, T.Yubisui, K.Shirabe, M.Takeshita, and A.Nakagawa (2004).
Structure of human erythrocyte NADH-cytochrome b5 reductase.
  Acta Crystallogr D Biol Crystallogr, 60, 1929-1934.
PDB code: 1umk
14596603 A.R.Dewanti, and B.Mitra (2003).
A transient intermediate in the reaction catalyzed by (S)-mandelate dehydrogenase from Pseudomonas putida.
  Biochemistry, 42, 12893-12901.  
12919327 H.Minagawa, J.Shimada, and H.Kaneko (2003).
Effect of mutations at Glu160 and Val198 on the thermostability of lactate oxidase.
  Eur J Biochem, 270, 3628-3633.  
14595396 M.Esaki, T.Kanamori, S.Nishikawa, I.Shin, P.G.Schultz, and T.Endo (2003).
Tom40 protein import channel binds to non-native proteins and prevents their aggregation.
  Nat Struct Biol, 10, 988-994.  
14690431 P.Sobrado, and P.F.Fitzpatrick (2003).
Solvent and primary deuterium isotope effects show that lactate CH and OH bond cleavages are concerted in Y254F flavocytochrome b2, consistent with a hydride transfer mechanism.
  Biochemistry, 42, 15208-15214.  
  12537557 W.Mifsud, and A.Bateman (2002).
Membrane-bound progesterone receptors contain a cytochrome b5-like ligand-binding domain.
  Genome Biol, 3, RESEARCH0068.  
11377202 C.Breithaupt, J.Strassner, U.Breitinger, R.Huber, P.Macheroux, A.Schaller, and T.Clausen (2001).
X-ray structure of 12-oxophytodienoate reductase 1 provides structural insight into substrate binding and specificity within the family of OYE.
  Structure, 9, 419-429.
PDB codes: 1icp 1icq 1ics
11230118 J.H.Lim, F.Martin, B.Guiard, N.Pfanner, and W.Voos (2001).
The mitochondrial Hsp70-dependent import system actively unfolds preproteins and shortens the lag phase of translocation.
  EMBO J, 20, 941-950.  
11559361 M.Gondry, J.Dubois, M.Terrier, and F.Lederer (2001).
The catalytic role of tyrosine 254 in flavocytochrome b2 (L-lactate dehydrogenase from baker's yeast). Comparison between the Y254F and Y254L mutant proteins.
  Eur J Biochem, 268, 4918-4927.  
11559365 M.Roncel, J.M.Ortega, and M.Losada (2001).
Factors determining the special redox properties of photosynthetic cytochrome b559.
  Eur J Biochem, 268, 4961-4968.  
11170421 P.Sobrado, S.C.Daubner, and P.F.Fitzpatrick (2001).
Probing the relative timing of hydrogen abstraction steps in the flavocytochrome b2 reaction with primary and solvent deuterium isotope effects and mutant enzymes.
  Biochemistry, 40, 994.  
10673428 B.M.Hallberg, T.Bergfors, K.Bäckbro, G.Pettersson, G.Henriksson, and C.Divne (2000).
A new scaffold for binding haem in the cytochrome domain of the extracellular flavocytochrome cellobiose dehydrogenase.
  Structure, 8, 79-88.
PDB codes: 1d7b 1d7c 1d7d
10727218 C.G.Mowat, I.Beaudoin, R.C.Durley, J.D.Barton, A.D.Pike, Z.W.Chen, G.A.Reid, S.K.Chapman, F.S.Mathews, and F.Lederer (2000).
Kinetic and crystallographic studies on the active site Arg289Lys mutant of flavocytochrome b2 (yeast L-lactate dehydrogenase).
  Biochemistry, 39, 3266-3275.
PDB code: 1qcw
11106776 D.F.Lewis, and P.Hlavica (2000).
Interactions between redox partners in various cytochrome P450 systems: functional and structural aspects.
  Biochim Biophys Acta, 1460, 353-374.  
10931200 G.Fleischmann, F.Lederer, F.Müller, A.Bacher, and H.Rüterjans (2000).
Flavin-protein interactions in flavocytochrome b2 as studied by NMR after reconstitution of the enzyme with 13C- and 15N-labelled flavin.
  Eur J Biochem, 267, 5156-5167.  
10653664 G.Gadda, A.Banerjee, and P.F.Fitzpatrick (2000).
Identification of an essential tyrosine residue in nitroalkane oxidase by modification with tetranitromethane.
  Biochemistry, 39, 1162-1168.  
10684621 G.Gadda, and P.F.Fitzpatrick (2000).
Mechanism of nitroalkane oxidase: 2. pH and kinetic isotope effects.
  Biochemistry, 39, 1406-1410.  
10955993 I.E.Lehoux, and B.Mitra (2000).
Role of arginine 277 in (S)-mandelate dehydrogenase from Pseudomonas putida in substrate binding and transition state stabilization.
  Biochemistry, 39, 10055-10065.  
10842340 J.Wu, J.H.Gan, Z.X.Xia, Y.H.Wang, W.H.Wang, L.L.Xue, Y.Xie, and Z.X.Huang (2000).
Crystal structure of recombinant trypsin-solubilized fragment of cytochrome b(5) and the structural comparison with Val61His mutant.
  Proteins, 40, 249-257.
PDB codes: 1ehb 1es1
10706608 K.Yorita, H.Misaki, B.A.Palfey, and V.Massey (2000).
On the interpretation of quantitative structure-function activity relationship data for lactate oxidase.
  Proc Natl Acad Sci U S A, 97, 2480-2485.  
11078532 K.Yorita, T.Matsuoka, H.Misaki, and V.Massey (2000).
Interaction of two arginine residues in lactate oxidase with the enzyme flavin: conversion of FMN to 8-formyl-FMN.
  Proc Natl Acad Sci U S A, 97, 13039-13044.  
10944103 P.D.Pawelek, J.Cheah, R.Coulombe, P.Macheroux, S.Ghisla, and A.Vrielink (2000).
The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site.
  EMBO J, 19, 4204-4215.
PDB codes: 1f8r 1f8s
10869173 P.Trickey, J.Basran, L.Y.Lian, Z.Chen, J.D.Barton, M.J.Sutcliffe, N.S.Scrutton, and F.S.Mathews (2000).
Structural and biochemical characterization of recombinant wild type and a C30A mutant of trimethylamine dehydrogenase from methylophilus methylotrophus (sp. W(3)A(1)).
  Biochemistry, 39, 7678-7688.
PDB codes: 1djn 1djq
10231535 I.E.Lehoux, and B.Mitra (1999).
(S)-Mandelate dehydrogenase from Pseudomonas putida: mechanistic studies with alternate substrates and pH and kinetic isotope effects.
  Biochemistry, 38, 5836-5848.  
10593892 I.F.Sevrioukova, J.T.Hazzard, G.Tollin, and T.L.Poulos (1999).
The FMN to heme electron transfer in cytochrome P450BM-3. Effect of chemical modification of cysteines engineered at the FMN-heme domain interaction site.
  J Biol Chem, 274, 36097-36106.  
10092614 K.M.Fox, and P.A.Karplus (1999).
The flavin environment in old yellow enzyme. An evaluation of insights from spectroscopic and artificial flavin studies.
  J Biol Chem, 274, 9357-9362.  
10428797 S.A.Sanders, C.H.Williams, and V.Massey (1999).
The roles of two amino acid residues in the active site of L-lactate monooxygenase. Mutation of arginine 187 to methionine and histidine 240 to glutamine.
  J Biol Chem, 274, 22289-22295.  
10585439 V.Kostanjevecki, D.Leys, G.Van Driessche, T.E.Meyer, M.A.Cusanovich, U.Fischer, Y.Guisez, and J.Van Beeumen (1999).
Structure and characterization of Ectothiorhodospira vacuolata cytochrome b(558), a prokaryotic homologue of cytochrome b(5).
  J Biol Chem, 274, 35614-35620.
PDB code: 1cxy
9822595 B.Gaume, C.Klaus, C.Ungermann, B.Guiard, W.Neupert, and M.Brunner (1998).
Unfolding of preproteins upon import into mitochondria.
  EMBO J, 17, 6497-6507.  
9521665 C.S.Miles, F.Lederer, and K.H.Lê (1998).
Probing intramolecular electron transfer within flavocytochrome b2 with a monoclonal antibody.
  Biochemistry, 37, 3440-3448.  
9558355 G.Gadda, and P.F.Fitzpatrick (1998).
Biochemical and physical characterization of the active FAD-containing form of nitroalkane oxidase from Fusarium oxysporum.
  Biochemistry, 37, 6154-6164.  
9772189 G.J.Mancini-Samuelson, V.Kieweg, K.M.Sabaj, S.Ghisla, and M.T.Stankovich (1998).
Redox properties of human medium-chain acyl-CoA dehydrogenase, modulation by charged active-site amino acid residues.
  Biochemistry, 37, 14605-14612.  
  9684885 K.S.Rao, and F.Lederer (1998).
About the pKa of the active-site histidine in flavocytochrome b2 (yeast L-lactate dehydrogenase).
  Protein Sci, 7, 1531-1537.  
9723208 M.Enescu, L.Lindqvist, and B.Soep (1998).
Excited-state dynamics of fully reduced flavins and flavoenzymes studied at subpicosecond time resolution.
  Photochem Photobiol, 68, 150-156.  
9737853 M.Tegoni, M.C.Silvestrini, B.Guigliarelli, M.Asso, M.Brunori, and P.Bertrand (1998).
Temperature-jump and potentiometric studies on recombinant wild type and Y143F and Y254F mutants of Saccharomyces cerevisiae flavocytochrome b2: role of the driving force in intramolecular electron transfer kinetics.
  Biochemistry, 37, 12761-12771.  
9434899 A.Mattevi, M.A.Vanoni, and B.Curti (1997).
Structure of D-amino acid oxidase: new insights from an old enzyme.
  Curr Opin Struct Biol, 7, 804-810.  
  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
9016724 J.C.Eads, D.Ozturk, T.B.Wexler, C.Grubmeyer, and J.C.Sacchettini (1997).
A new function for a common fold: the crystal structure of quinolinic acid phosphoribosyltransferase.
  Structure, 5, 47-58.
PDB code: 1qap
9230706 J.R.Albani (1997).
Interaction between cytochrome b2 core and flavodehydrogenase from the yeast Hansenula anomala.
  Photochem Photobiol, 66, 72-75.  
8999912 K.Ratnam, N.Shiraishi, W.H.Campbell, and R.Hille (1997).
Spectroscopic and kinetic characterization of the recombinant cytochrome c reductase fragment of nitrate reductase. Identification of the rate-limiting catalytic step.
  J Biol Chem, 272, 2122-2128.  
9275167 K.Yorita, K.Janko, K.Aki, S.Ghisla, B.A.Palfey, and V.Massey (1997).
On the reaction mechanism of L-lactate oxidase: quantitative structure-activity analysis of the reaction with para-substituted L-mandelates.
  Proc Natl Acad Sci U S A, 94, 9590-9595.  
9220981 M.Tegoni, M.Gervais, and A.Desbois (1997).
Resonance Raman study on the oxidized and anionic semiquinone forms of flavocytochrome b2 and L-lactate monooxygenase. Influence of the structure and environment of the isoalloxazine ring on the flavin function.
  Biochemistry, 36, 8932-8946.  
9188703 N.Izadi, Y.Henry, J.Haladjian, M.E.Goldberg, C.Wandersman, M.Delepierre, and A.Lecroisey (1997).
Purification and characterization of an extracellular heme-binding protein, HasA, involved in heme iron acquisition.
  Biochemistry, 36, 7050-7057.  
9188712 N.Rouvière, M.Mayer, M.Tegoni, C.Capeillère-Blandin, and F.Lederer (1997).
Molecular interpretation of inhibition by excess substrate in flavocytochrome b2: a study with wild-type and Y143F mutant enzymes.
  Biochemistry, 36, 7126-7135.  
9032071 P.Rowland, F.S.Nielsen, K.F.Jensen, and S.Larsen (1997).
The crystal structure of the flavin containing enzyme dihydroorotate dehydrogenase A from Lactococcus lactis.
  Structure, 5, 239-252.
PDB code: 1dor
9341146 W.Sun, C.H.Williams, and V.Massey (1997).
The role of glycine 99 in L-lactate monooxygenase from Mycobacterium smegmatis.
  J Biol Chem, 272, 27065-27076.  
8706682 A.Belmouden, and F.Lederer (1996).
The role of a beta barrel loop 4 extension in modulating the physical and functional properties of long-chain 2-hydroxy-acid oxidase isozymes.
  Eur J Biochem, 238, 790-798.  
8703001 A.J.Fisher, T.B.Thompson, J.B.Thoden, T.O.Baldwin, and I.Rayment (1996).
The 1.5-A resolution crystal structure of bacterial luciferase in low salt conditions.
  J Biol Chem, 271, 21956-21968.
PDB code: 1luc
8755502 A.Mattevi, M.A.Vanoni, F.Todone, M.Rizzi, A.Teplyakov, A.Coda, M.Bolognesi, and B.Curti (1996).
Crystal structure of D-amino acid oxidase: a case of active site mirror-image convergent evolution with flavocytochrome b2.
  Proc Natl Acad Sci U S A, 93, 7496-7501.
PDB code: 1kif
8880927 H.Nishida, and K.Miki (1996).
Electrostatic properties deduced from refined structures of NADH-cytochrome b5 reductase and the other flavin-dependent reductases: pyridine nucleotide-binding and interaction with an electron-transfer partner.
  Proteins, 26, 32-41.  
8910450 K.Yorita, K.Aki, T.Ohkuma-Soyejima, T.Kokubo, H.Misaki, and V.Massey (1996).
Conversion of L-lactate oxidase to a long chain alpha-hydroxyacid oxidase by site-directed mutagenesis of alanine 95 to glycine.
  J Biol Chem, 271, 28300-28305.  
8679620 M.Gondry, and F.Lederer (1996).
Functional properties of the histidine-aspartate ion pair of flavocytochrome b2 (L-lactate dehydrogenase): substitution of Asp282 with asparagine.
  Biochemistry, 35, 8587-8594.  
8547270 R.E.Sharp, S.K.Chapman, and G.A.Reid (1996).
Deletions in the interdomain hinge region of flavocytochrome b2: effects on intraprotein electron transfer.
  Biochemistry, 35, 891-899.  
8639579 S.Daff, W.J.Ingledew, G.A.Reid, and S.K.Chapman (1996).
New insights into the catalytic cycle of flavocytochrome b2.
  Biochemistry, 35, 6345-6350.  
  8819171 S.Govindaraj, and T.L.Poulos (1996).
Probing the structure of the linker connecting the reductase and heme domains of cytochrome P450BM-3 using site-directed mutagenesis.
  Protein Sci, 5, 1389-1393.  
  8762144 S.Janecek (1996).
Invariant glycines and prolines flanking in loops the strand beta 2 of various (alpha/beta)8-barrel enzymes: a hidden homology?
  Protein Sci, 5, 1136-1143.  
8663383 W.Sun, C.H.Williams, and V.Massey (1996).
Site-directed mutagenesis of glycine 99 to alanine in L-lactate monooxygenase from Mycobacterium smegmatis.
  J Biol Chem, 271, 17226-17233.  
  8654364 W.Voos, O.von Ahsen, H.Müller, B.Guiard, J.Rassow, and N.Pfanner (1996).
Differential requirement for the mitochondrial Hsp70-Tim44 complex in unfolding and translocation of preproteins.
  EMBO J, 15, 2668-2677.  
8710874 Z.Y.Zhu, and S.Karlin (1996).
Clusters of charged residues in protein three-dimensional structures.
  Proc Natl Acad Sci U S A, 93, 8350-8355.  
8847340 C.C.Moser, C.C.Page, R.Farid, and P.L.Dutton (1995).
Biological electron transfer.
  J Bioenerg Biomembr, 27, 263-274.  
  7645302 D.F.Lewis (1995).
Three-dimensional models of human and other mammalian microsomal P450s constructed from an alignment with P450102 (P450bm3).
  Xenobiotica, 25, 333-366.  
  7663348 M.Gondry, K.H.Diêp Lê, F.D.Manson, S.K.Chapman, F.S.Mathews, G.A.Reid, and F.Lederer (1995).
On the lack of coordination between protein folding and flavin insertion in Escherichia coli for flavocytochrome b2 mutant forms Y254L and D282N.
  Protein Sci, 4, 925-935.  
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.  
  8563637 R.M.Stroud, and E.B.Fauman (1995).
Significance of structural changes in proteins: expected errors in refined protein structures.
  Protein Sci, 4, 2392-2404.  
8749369 T.O.Baldwin, J.A.Christopher, F.M.Raushel, J.F.Sinclair, M.M.Ziegler, A.J.Fisher, and I.Rayment (1995).
Structure of bacterial luciferase.
  Curr Opin Struct Biol, 5, 798-809.  
8592705 T.Sandalova, and Y.Lindqvist (1995).
Three-dimensional model of the alpha-subunit of bacterial luciferase.
  Proteins, 23, 241-255.  
  8557026 U.Ermler, R.A.Siddiqui, R.Cramm, and B.Friedrich (1995).
Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 A resolution.
  EMBO J, 14, 6067-6077.
PDB code: 1cqx
  8142887 A.Balme, and F.Lederer (1994).
On the rate of proton exchange with solvent of the catalytic histidine in flavocytochrome b2 (yeast L-lactate dehydrogenase).
  Protein Sci, 3, 109-117.  
7881908 K.M.Fox, and P.A.Karplus (1994).
Old yellow enzyme at 2 A resolution: overall structure, ligand binding, and comparison with related flavoproteins.
  Structure, 2, 1089-1105.
PDB codes: 1oya 1oyb 1oyc
  8003966 M.Tegoni, and C.Cambillau (1994).
The 2.6-A refined structure of the Escherichia coli recombinant Saccharomyces cerevisiae flavocytochrome b2-sulfite complex.
  Protein Sci, 3, 303-313.
PDB code: 1ltd
8119302 R.A.Stuart, A.Gruhler, I.van der Klei, B.Guiard, H.Koll, and W.Neupert (1994).
The requirement of matrix ATP for the import of precursor proteins into the mitochondrial matrix and intermembrane space.
  Eur J Biochem, 220, 9.  
8160272 R.A.Stuart, D.M.Cyr, E.A.Craig, and W.Neupert (1994).
Mitochondrial molecular chaperones: their role in protein translocation.
  Trends Biochem Sci, 19, 87-92.  
7988658 R.A.Stuart, D.M.Cyr, and W.Neupert (1994).
Hsp70 in mitochondrial biogenesis: from chaperoning nascent polypeptide chains to facilitation of protein degradation.
  Experientia, 50, 1002-1011.  
8060489 S.L.Alam, J.D.Satterlee, and C.G.Edmonds (1994).
Complete amino acid sequence of the Glycera dibranchiata monomer hemoglobin component IV: structural implications.
  J Protein Chem, 13, 151-164.  
  7849601 W.R.Taylor, T.P.Flores, and C.A.Orengo (1994).
Multiple protein structure alignment.
  Protein Sci, 3, 1858-1870.  
8508789 A.Belmouden, K.H.Lê, F.Lederer, and H.J.Garchon (1993).
Molecular cloning and nucleotide sequence of cDNA encoding rat kidney long-chain L-2-hydroxy acid oxidase. Expression of the catalytically active recombinant protein as a chimaera.
  Eur J Biochem, 214, 17-25.  
  8268801 B.S.Glick, C.Wachter, G.A.Reid, and G.Schatz (1993).
Import of cytochrome b2 to the mitochondrial intermembrane space: the tightly folded heme-binding domain makes import dependent upon matrix ATP.
  Protein Sci, 2, 1901-1917.  
  8382992 L.Chen, F.S.Mathews, V.L.Davidson, M.Tegoni, C.Rivetti, and G.L.Rossi (1993).
Preliminary crystal structure studies of a ternary electron transfer complex between a quinoprotein, a blue copper protein, and a c-type cytochrome.
  Protein Sci, 2, 147-154.  
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.  
8433995 M.Wilmanns, and D.Eisenberg (1993).
Three-dimensional profiles from residue-pair preferences: identification of sequences with beta/alpha-barrel fold.
  Proc Natl Acad Sci U S A, 90, 1379-1383.  
8504801 P.Macheroux, V.Kieweg, V.Massey, E.Söderlind, K.Stenberg, and Y.Lindqvist (1993).
Role of tyrosine 129 in the active site of spinach glycolate oxidase.
  Eur J Biochem, 213, 1047-1054.  
8408192 W.Voos, B.D.Gambill, B.Guiard, N.Pfanner, and E.A.Craig (1993).
Presequence and mature part of preproteins strongly influence the dependence of mitochondrial protein import on heat shock protein 70 in the matrix.
  J Cell Biol, 123, 119-126.  
  1338973 F.Lederer (1992).
Extreme pKa displacements at the active sites of FMN-dependent alpha-hydroxy acid-oxidizing enzymes.
  Protein Sci, 1, 540-548.  
1470679 J.E.Walker (1992).
The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains.
  Q Rev Biophys, 25, 253-324.  
1409561 R.P.Sheridan, and R.Venkataraghavan (1992).
A systematic search for protein signature sequences.
  Proteins, 14, 16-28.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

spacer
spacer