PDBsum entry 1ccc

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Oxidoreductase PDB id
Protein chain
291 a.a. *
Waters ×51
* Residue conservation analysis
PDB id:
Name: Oxidoreductase
Title: The asp-his-fe triad of cytochromE C peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free-radical to the heme
Structure: CytochromE C peroxidase. Chain: a. Engineered: yes
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932
2.00Å     R-factor:   0.190    
Authors: D.B.Goodin,D.E.Mcree
Key ref:
D.B.Goodin and D.E.McRee (1993). The Asp-His-Fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free radical to the heme. Biochemistry, 32, 3313-3324. PubMed id: 8384877 DOI: 10.1021/bi00064a014
04-Jan-93     Release date:   31-Oct-93    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P00431  (CCPR_YEAST) -  Cytochrome c peroxidase, mitochondrial
361 a.a.
291 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.  - 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
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!
  Biological process     oxidation-reduction process   2 terms 
  Biochemical function     peroxidase activity     2 terms  


DOI no: 10.1021/bi00064a014 Biochemistry 32:3313-3324 (1993)
PubMed id: 8384877  
The Asp-His-Fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free radical to the heme.
D.B.Goodin, D.E.McRee.
The buried charge of Asp-235 in cytochrome c peroxidase (CCP) forms an important hydrogen bond to the histidine ligand of the heme iron. The Asp-His-metal interaction, which is similar to the catalytic triad of serine proteases, is found at the active site of many metalloenzymes and is believed to modulate the character of histidine as a metal ligand. We have examined the influence of this interaction in CCP on the function, redox properties, and iron zero-field splitting in the native ferric state and its effect on the Trp-191 free radical site in the oxidized ES complex. Unlike D235A and D235N, the mutation D235E introduces very little perturbation in the X-ray crystal structure of the enzyme active site, with only minor changes in the geometry of the carboxylate-histidine interaction and no observable change at the Trp-191 free radical site. More significant effects are observed in the position of the helix containing residue Glu-235. However, the small change in hydrogen bond geometry is all that is necessary to (1) increase the reduction potential by 70 mV, (2) alter the anisotropy of the Trp-191 free radical EPR, (3) affect the activity and spin-state equilibrium, and (4) reduce the strength of the iron ligand field as measured by the zero-field splitting. The changes in the redox potential with substitution are correlated with the observed zero-field splitting, suggesting that redox control is exerted through the heme ligand by a combination of electrostatic and ligand field effects. The replacement of Asp-235 with Glu appears to result in a significantly weaker hydrogen bond in which the proton resides essentially with His-175. This hydrogen bond is nevertheless strong enough to prevent the reorientation of Trp-191 and the conversion to one of two low-spin states observed for D235A and D235N. The Asp-His-Fe interaction is therefore as important in defining the redox properties and imidazolate character of His-175 as has been proposed, yet its most important role in peroxidase function may be to correctly orient Trp-191 for efficient coupling of the free radical to the heme and to maintain a high-spin 5-coordinate heme center.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21334283 C.M.DiCarlo, L.B.Vitello, and J.E.Erman (2011).
Reduction potential of yeast cytochrome c peroxidase and three distal histidine mutants: dependence on pH.
  J Inorg Biochem, 105, 532-537.  
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
20445228 Serrano, J.D'Antonio, S.Franzen, and R.A.Ghiladi (2010).
Structure of dehaloperoxidase B at 1.58 A resolution and structural characterization of the AB dimer from Amphitrite ornata.
  Acta Crystallogr D Biol Crystallogr, 66, 529-538.
PDB code: 3ixf
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
19129158 S.Jokipii-Lukkari, A.D.Frey, P.T.Kallio, and H.Häggman (2009).
Intrinsic non-symbiotic and truncated haemoglobins and heterologous Vitreoscilla haemoglobin expression in plants.
  J Exp Bot, 60, 409-422.  
18923851 S.W.Vetter, A.C.Terentis, R.L.Osborne, J.H.Dawson, and D.B.Goodin (2009).
Replacement of the axial histidine heme ligand with cysteine in nitrophorin 1: spectroscopic and crystallographic characterization.
  J Biol Inorg Chem, 14, 179-191.  
19865536 V.Daskalakis, and C.Varotsis (2009).
Binding and Docking Interactions of NO, CO and O(2) in Heme Proteins as Probed by Density Functional Theory.
  Int J Mol Sci, 10, 4137-4156.  
19252222 V.Rauhamäki, D.A.Bloch, M.I.Verkhovsky, and M.Wikström (2009).
Active Site of Cytochrome cbb3.
  J Biol Chem, 284, 11301-11308.  
17665226 B.N.Hudder, J.G.Morales, A.Stubna, E.Münck, M.P.Hendrich, and P.A.Lindahl (2007).
Electron paramagnetic resonance and Mössbauer spectroscopy of intact mitochondria from respiring Saccharomyces cerevisiae.
  J Biol Inorg Chem, 12, 1029-1053.  
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.  
17654547 C.Zubieta, R.Joseph, S.S.Krishna, D.McMullan, M.Kapoor, H.L.Axelrod, M.D.Miller, P.Abdubek, C.Acosta, T.Astakhova, D.Carlton, H.J.Chiu, T.Clayton, M.C.Deller, L.Duan, Y.Elias, M.A.Elsliger, J.Feuerhelm, S.K.Grzechnik, J.Hale, G.W.Han, L.Jaroszewski, K.K.Jin, H.E.Klock, M.W.Knuth, P.Kozbial, A.Kumar, D.Marciano, A.T.Morse, K.D.Murphy, E.Nigoghossian, L.Okach, S.Oommachen, R.Reyes, C.L.Rife, P.Schimmel, C.V.Trout, H.van den Bedem, D.Weekes, A.White, Q.Xu, K.O.Hodgson, J.Wooley, A.M.Deacon, A.Godzik, S.A.Lesley, and I.A.Wilson (2007).
Identification and structural characterization of heme binding in a novel dye-decolorizing peroxidase, TyrA.
  Proteins, 69, 234-243.
PDB code: 2iiz
17654545 C.Zubieta, S.S.Krishna, M.Kapoor, P.Kozbial, D.McMullan, H.L.Axelrod, M.D.Miller, P.Abdubek, E.Ambing, T.Astakhova, D.Carlton, H.J.Chiu, T.Clayton, M.C.Deller, L.Duan, M.A.Elsliger, J.Feuerhelm, S.K.Grzechnik, J.Hale, E.Hampton, G.W.Han, L.Jaroszewski, K.K.Jin, H.E.Klock, M.W.Knuth, A.Kumar, D.Marciano, A.T.Morse, E.Nigoghossian, L.Okach, S.Oommachen, R.Reyes, C.L.Rife, P.Schimmel, H.van den Bedem, D.Weekes, A.White, Q.Xu, K.O.Hodgson, J.Wooley, A.M.Deacon, A.Godzik, S.A.Lesley, and I.A.Wilson (2007).
Crystal structures of two novel dye-decolorizing peroxidases reveal a beta-barrel fold with a conserved heme-binding motif.
  Proteins, 69, 223-233.
PDB codes: 2gvk 2hag
17900177 L.V.Michel, T.Ye, S.E.Bowman, B.D.Levin, M.A.Hahn, B.S.Russell, S.J.Elliott, and K.L.Bren (2007).
Heme attachment motif mobility tunes cytochrome c redox potential.
  Biochemistry, 46, 11753-11760.  
17031705 R.F.Abdelhamid, Y.Obara, Y.Uchida, T.Kohzuma, D.M.Dooley, D.E.Brown, and H.Hori (2007).
Pi-pi interaction between aromatic ring and copper-coordinated His81 imidazole regulates the blue copper active-site structure.
  J Biol Inorg Chem, 12, 165-173.  
17881827 Serrano, Z.Chen, M.F.Davis, and S.Franzen (2007).
X-ray crystal structural analysis of the binding site in the ferric and oxyferrous forms of the recombinant heme dehaloperoxidase cloned from Amphitrite ornata.
  Acta Crystallogr D Biol Crystallogr, 63, 1094-1101.
PDB codes: 2qfk 2qfn
17928290 Y.Sugano, R.Muramatsu, A.Ichiyanagi, T.Sato, and M.Shoda (2007).
DyP, a unique dye-decolorizing peroxidase, represents a novel heme peroxidase family: ASP171 replaces the distal histidine of classical peroxidases.
  J Biol Chem, 282, 36652-36658.  
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.  
15965735 A.Ebihara, A.Okamoto, Y.Kousumi, H.Yamamoto, R.Masui, N.Ueyama, S.Yokoyama, and S.Kuramitsu (2005).
Structure-based functional identification of a novel heme-binding protein from Thermus thermophilus HB8.
  J Struct Funct Genomics, 6, 21-32.
PDB code: 1vdh
16262691 B.D.Howes, N.C.Brissett, W.A.Doyle, A.T.Smith, and G.Smulevich (2005).
Spectroscopic and kinetic properties of the horseradish peroxidase mutant T171S. Evidence for selective effects on the reduced state of the enzyme.
  FEBS J, 272, 5514-5521.  
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.  
16133205 G.Battistuzzi, M.Bellei, M.Borsari, G.Di Rocco, A.Ranieri, and M.Sola (2005).
Axial ligation and polypeptide matrix effects on the reduction potential of heme proteins probed on their cyanide adducts.
  J Biol Inorg Chem, 10, 643-651.  
14550944 A.D.Frey, and P.T.Kallio (2003).
Bacterial hemoglobins and flavohemoglobins: versatile proteins and their impact on microbiology and biotechnology.
  FEMS Microbiol Rev, 27, 525-545.  
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.  
12618432 C.A.Cunha, S.Macieira, J.M.Dias, G.Almeida, L.L.Goncalves, C.Costa, J.Lampreia, R.Huber, J.J.Moura, I.Moura, and M.J.Romão (2003).
Cytochrome c nitrite reductase from Desulfovibrio desulfuricans ATCC 27774. The relevance of the two calcium sites in the structure of the catalytic subunit (NrfA).
  J Biol Chem, 278, 17455-17465.
PDB code: 1oah
11959963 E.N.Marsh, and W.F.DeGrado (2002).
Noncovalent self-assembly of a heterotetrameric diiron protein.
  Proc Natl Acad Sci U S A, 99, 5150-5154.  
12119039 H.A.Heering, C.Indiani, G.Regelsberger, C.Jakopitsch, C.Obinger, and G.Smulevich (2002).
New insights into the heme cavity structure of catalase-peroxidase: a spectroscopic approach to the recombinant synechocystis enzyme and selected distal cavity mutants.
  Biochemistry, 41, 9237-9247.  
12354119 S.Franzen, E.S.Peterson, D.Brown, J.M.Friedman, M.R.Thomas, and S.G.Boxer (2002).
Proximal ligand motions in H93G myoglobin.
  Eur J Biochem, 269, 4879-4886.  
12351682 S.R.Wilkinson, S.O.Obado, I.L.Mauricio, and J.M.Kelly (2002).
Trypanosoma cruzi expresses a plant-like ascorbate-dependent hemoperoxidase localized to the endoplasmic reticulum.
  Proc Natl Acad Sci U S A, 99, 13453-13458.  
11170453 J.Hirst, S.K.Wilcox, J.Ai, P.Moënne-Loccoz, T.M.Loehr, and D.B.Goodin (2001).
Replacement of the axial histidine ligand with imidazole in cytochrome c peroxidase. 2. Effects on heme coordination and function.
  Biochemistry, 40, 1274-1283.  
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
11371218 J.T.Lecomte, N.L.Scott, B.C.Vu, and C.J.Falzone (2001).
Binding of ferric heme by the recombinant globin from the cyanobacterium Synechocystis sp. PCC 6803.
  Biochemistry, 40, 6541-6552.  
11141052 R.A.Edwards, M.M.Whittaker, J.W.Whittaker, E.N.Baker, and G.B.Jameson (2001).
Outer sphere mutations perturb metal reactivity in manganese superoxide dismutase.
  Biochemistry, 40, 15-27.
PDB codes: 1en4 1en5 1en6
10722697 J.Hirst, and D.B.Goodin (2000).
Unusual oxidative chemistry of N(omega)-hydroxyarginine and N-hydroxyguanidine catalyzed at an engineered cavity in a heme peroxidase.
  J Biol Chem, 275, 8582-8591.
PDB codes: 1dj1 1dj5
10828979 S.A.Seibold, J.F.Cerda, A.M.Mulichak, I.Song, R.M.Garavito, T.Arakawa, W.L.Smith, and G.T.Babcock (2000).
Peroxidase activity in prostaglandin endoperoxide H synthase-1 occurs with a neutral histidine proximal heme ligand.
  Biochemistry, 39, 6616-6624.  
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
10606521 X.Wang, and G.J.Pielak (1999).
Equilibrium thermodynamics of a physiologically-relevant heme-protein complex.
  Biochemistry, 38, 16876-16881.  
9548935 C.K.Vance, and A.F.Miller (1998).
Spectroscopic comparisons of the pH dependencies of Fe-substituted (Mn)superoxide dismutase and Fe-superoxide dismutase.
  Biochemistry, 37, 5518-5527.  
9692324 F.Nastri, A.Lombardi, L.D.D'Andrea, M.Sanseverino, O.Maglio, and V.Pavone (1998).
Miniaturized hemoproteins.
  Biopolymers, 47, 5.  
9694851 M.Ekberg, S.Pötsch, E.Sandin, M.Thunnissen, P.Nordlund, M.Sahlin, and B.M.Sjöberg (1998).
Preserved catalytic activity in an engineered ribonucleotide reductase R2 protein with a nonphysiological radical transfer pathway. The importance of hydrogen bond connections between the participating residues.
  J Biol Chem, 273, 21003-21008.  
9485413 M.Tanaka, K.Ishimori, and I.Morishima (1998).
Structural roles of the highly conserved glu residue in the heme distal site of peroxidases.
  Biochemistry, 37, 2629-2638.  
  9765568 P.Bandyopadhyay, and H.M.Steinman (1998).
Legionella pneumophila catalase-peroxidases: cloning of the katB gene and studies of KatB function.
  J Bacteriol, 180, 5369-5374.  
9836578 S.K.Wilcox, C.D.Putnam, M.Sastry, J.Blankenship, W.J.Chazin, D.E.McRee, and D.B.Goodin (1998).
Rational design of a functional metalloenzyme: introduction of a site for manganese binding and oxidation into a heme peroxidase.
  Biochemistry, 37, 16853-16862.
PDB code: 1bva
  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
9033390 C.L.Hunter, E.Lloyd, L.D.Eltis, S.P.Rafferty, H.Lee, M.Smith, and A.G.Mauk (1997).
Role of the heme propionates in the interaction of heme with apomyoglobin and apocytochrome b5.
  Biochemistry, 36, 1010-1017.  
9100022 K.Kishi, D.P.Hildebrand, M.Kusters-van Someren, J.Gettemy, A.G.Mauk, and M.H.Gold (1997).
Site-directed mutations at phenylalanine-190 of manganese peroxidase: effects on stability, function, and coordination.
  Biochemistry, 36, 4268-4277.  
9220980 M.M.Whittaker, and J.W.Whittaker (1997).
Mutagenesis of a proton linkage pathway in Escherichia coli manganese superoxide dismutase.
  Biochemistry, 36, 8923-8931.  
9211904 M.Sundaramoorthy, K.Kishi, M.H.Gold, and T.L.Poulos (1997).
Crystal structures of substrate binding site mutants of manganese peroxidase.
  J Biol Chem, 272, 17574-17580.
PDB codes: 1mn1 1mn2
9245411 M.Tanaka, S.Nagano, K.Ishimori, and I.Morishima (1997).
Hydrogen bond network in the distal site of peroxidases: spectroscopic properties of Asn70 --> Asp horseradish peroxidase mutant.
  Biochemistry, 36, 9791-9798.  
9153405 S.Sarma, R.J.DiGate, D.B.Goodin, C.J.Miller, and R.D.Guiles (1997).
Effect of axial ligand plane reorientation on electronic and electrochemical properties observed in the A67V mutant of rat cytochrome b5.
  Biochemistry, 36, 5658-5668.  
8652584 B.He, R.Sinclair, B.R.Copeland, R.Makino, L.S.Powers, and I.Yamazaki (1996).
The structure-function relationship and reduction potentials of high oxidation states of myoglobin and peroxidase.
  Biochemistry, 35, 2413-2420.  
8910568 D.E.Holloway, H.P.Chen, and E.N.Marsh (1996).
Carboxymethylation of MutS-cysteine-15 specifically inactivates adenosylcobalamin-dependent glutamate mutase. Examination of the role of this residue in coenzyme-binding and catalysis.
  J Biol Chem, 271, 29121-29125.  
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.  
8652589 M.Amaratunga, K.Fluhr, J.T.Jarrett, C.L.Drennan, M.L.Ludwig, R.G.Matthews, and J.D.Scholten (1996).
A synthetic module for the metH gene permits facile mutagenesis of the cobalamin-binding region of Escherichia coli methionine synthase: initial characterization of seven mutant proteins.
  Biochemistry, 35, 2453-2463.  
8916924 N.C.Veitch, Y.Gao, and K.G.Welinder (1996).
The Asp245-->Asn mutant of Coprinus cinereus peroxidase. Characterization by 1H-NMR spectroscopy and comparison with the wild-type enzyme.
  Biochemistry, 35, 14370-14380.  
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
8841121 S.L.Newmyer, J.Sun, T.M.Loehr, and P.R.Ortiz de Montellano (1996).
Rescue of the horseradish peroxidase His-170-->Ala mutant activity by imidazole: importance of proximal ligand tethering.
  Biochemistry, 35, 12788-12795.  
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.  
  8528082 M.M.Fitzgerald, M.L.Trester, G.M.Jensen, D.E.McRee, and D.B.Goodin (1995).
The role of aspartate-235 in the binding of cations to an artificial cavity at the radical site of cytochrome c peroxidase.
  Protein Sci, 4, 1844-1850.
PDB codes: 1cmt 1cmu
7608169 M.R.Gunther, D.J.Kelman, J.T.Corbett, and R.P.Mason (1995).
Self-peroxidation of metmyoglobin results in formation of an oxygen-reactive tryptophan-centered radical.
  J Biol Chem, 270, 16075-16081.  
7759477 M.Sahlin, G.Lassmann, S.Pötsch, B.M.Sjöberg, and A.Gräslund (1995).
Transient free radicals in iron/oxygen reconstitution of mutant protein R2 Y122F. Possible participants in electron transfer chains in ribonucleotide reductase.
  J Biol Chem, 270, 12361-12372.  
7743126 P.R.Evans (1995).
A tail of B12 binding.
  Structure, 3, 121-122.  
  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
7629167 V.P.Miller, D.B.Goodin, A.E.Friedman, C.Hartmann, and P.R.Ortiz de Montellano (1995).
Horseradish peroxidase Phe172-->Tyr mutant. Sequential formation of compound I with a porphyrin radical cation and a protein radical.
  J Biol Chem, 270, 18413-18419.  
7712296 C.L.Drennan, R.G.Matthews, and M.L.Ludwig (1994).
Cobalamin-dependent methionine synthase: the structure of a methylcobalamin-binding fragment and implications for other B12-dependent enzymes.
  Curr Opin Struct Biol, 4, 919-929.  
7809133 D.E.McRee, G.M.Jensen, M.M.Fitzgerald, H.A.Siegel, and D.B.Goodin (1994).
Construction of a bisaquo heme enzyme and binding by exogenous ligands.
  Proc Natl Acad Sci U S A, 91, 12847-12851.
PDB codes: 1cce 1ccg
8168535 H.Le Moual, N.Dion, B.P.Roques, P.Crine, and G.Boileau (1994).
Asp650 is crucial for catalytic activity of neutral endopeptidase 24-11.
  Eur J Biochem, 221, 475-480.  
7764068 T.L.Poulos (1993).
  Curr Opin Biotechnol, 4, 484-489.  
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.