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PDBsum entry 1h5c
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Oxidoreductase PDB id
1h5c

 

 

 

 

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Contents
Protein chain
306 a.a. *
Ligands
HEM
ACT
Metals
_CA ×2
Waters ×420
* Residue conservation analysis
PDB id:
1h5c
Name: Oxidoreductase
Title: X-ray induced reduction of horseradish peroxidase c1a compound iii (100-200% dose)
Structure: Peroxidase c1a. Chain: a. Engineered: yes
Source: Armoracia rusticana. Horseradish. Organism_taxid: 3704. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: synthetic gene
Resolution:
1.62Å     R-factor:   0.178     R-free:   0.198
Authors: G.I.Berglund,G.H.Carlsson,J.Hajdu,A.T.Smith,H.Szoke,A.Henriksen
Key ref:
G.I.Berglund et al. (2002). The catalytic pathway of horseradish peroxidase at high resolution. Nature, 417, 463-468. PubMed id: 12024218 DOI: 10.1038/417463a
Date:
21-May-01     Release date:   18-Jun-02    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00433  (PER1A_ARMRU) -  Peroxidase C1A from Armoracia rusticana
Seq:
Struc: 		353 a.a.
306 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.11.1.7  - peroxidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
2 × a phenolic donor
 + H2O2
 = 2 × a phenolic radical donor
 + 2 × H2O
      Cofactor: Heme
Heme
Bound ligand (Het Group name = HEM) matches with 95.45% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
DOI no: 10.1038/417463a Nature 417:463-468 (2002)
PubMed id: 12024218  
 
 
The catalytic pathway of horseradish peroxidase at high resolution.
G.I.Berglund, G.H.Carlsson, A.T.Smith, H.Szöke, A.Henriksen, J.Hajdu.
 
  ABSTRACT  
 
A molecular description of oxygen and peroxide activation in biological systems is difficult, because electrons liberated during X-ray data collection reduce the active centres of redox enzymes catalysing these reactions. Here we describe an effective strategy to obtain crystal structures for high-valency redox intermediates and present a three-dimensional movie of the X-ray-driven catalytic reduction of a bound dioxygen species in horseradish peroxidase (HRP). We also describe separate experiments in which high-resolution structures could be obtained for all five oxidation states of HRP, showing such structures with preserved redox states for the first time.
 
  Selected figure(s)  
 
Figure 1.
Figure 1: The five oxidation states of horseradish peroxidase. 		Figure 4.
Figure 4: Spectra and refined high-resolution structures for the five oxidation states of horseradish peroxidase. Accession codes are shown. The structures were captured at high concentrations in individual experiments (Methods) and were obtained from the first few degrees of data (Table 2 of the Supplementary Information). a, Ferric enzyme. b, Ferrous enzyme. c, Compound III (Fe -O bond distance, 1.8 Å). d, Compound I (Fe -O bond distance, 1.7 Å). e, Compound II (Fe -O bond distance, 1.8 Å). SigmaA-weighted^30 2mF[obs] -DF[calc] maps contoured at 1 .
 
  The above figures are reprinted by permission from Macmillan Publishers Ltd: Nature (2002, 417, 463-468) copyright 2002.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21525643 A.M.Orville, R.Buono, M.Cowan, A.Héroux, G.Shea-McCarthy, D.K.Schneider, J.M.Skinner, M.J.Skinner, D.Stoner-Ma, and R.M.Sweet (2011).
Correlated single-crystal electronic absorption spectroscopy and X-ray crystallography at NSLS beamline X26-C.
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21525641 C.Homer, L.Cooper, and A.Gonzalez (2011).
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21525640 D.H.Juers, and M.Weik (2011).
Similarities and differences in radiation damage at 100 K versus 160 K in a crystal of thermolysin.
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21525644 R.L.Owen, B.A.Yorke, J.A.Gowdy, and A.R.Pearson (2011).
Revealing low-dose radiation damage using single-crystal spectroscopy.
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21034361 T.M.Cheng, S.J.Mao, S.T.Lai, C.C.Chang, M.C.Yang, N.C.Chen, S.C.Chou, and J.P.Pan (2011).
Haemoglobin-induced oxidative stress is associated with both endogenous peroxidase activity and H(2)O(2) generation from polyunsaturated fatty acids.
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21478616 Y.Wang, and Y.Hasebe (2011).
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20192189 C.Hu, C.D.Sulok, F.Paulat, N.Lehnert, A.I.Twigg, M.P.Hendrich, C.E.Schulz, and W.R.Scheidt (2010).
Just a proton: distinguishing the two electronic states of five-coordinate high-spin iron(II) porphyrinates with imidazole/ate coordination.
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20382986 E.F.Garman (2010).
Radiation damage in macromolecular crystallography: what is it and why should we care?
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Ultrahigh-throughput screening in drop-based microfluidics for directed evolution.
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20382998 M.Schiltz, and G.Bricogne (2010).
;Broken symmetries' in macromolecular crystallography: phasing from unmerged data.
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20382997 M.Weik, and J.P.Colletier (2010).
Temperature-dependent macromolecular X-ray crystallography.
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Raman-assisted crystallography suggests a mechanism of X-ray-induced disulfide radical formation and reparation.
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PDB codes: 2xbr 2xbs
20164644 S.Westenhoff, E.Nazarenko, E.Malmerberg, J.Davidsson, G.Katona, and R.Neutze (2010).
Time-resolved structural studies of protein reaction dynamics: a smorgasbord of X-ray approaches.
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20396396 Y.Yoshioka, and M.Mitani (2010).
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20437497 Z.Chen, L.Xu, Y.Liang, and M.Zhao (2010).
pH-Sensitive Water-Soluble Nanospheric Imprinted Hydrogels Prepared as Horseradish Peroxidase Mimetic Enzymes.
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Crystallization and preliminary X-ray diffraction of chlorite dismutase from Dechloromonas aromatica RCB.
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19520834 B.Sjöblom, M.Polentarutti, and K.Djinovic-Carugo (2009).
Structural study of X-ray induced activation of carbonic anhydrase.
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PDB codes: 2vva 2vvb
19164527 H.Aoyama, K.Muramoto, K.Shinzawa-Itoh, K.Hirata, E.Yamashita, T.Tsukihara, T.Ogura, and S.Yoshikawa (2009).
A peroxide bridge between Fe and Cu ions in the O2 reduction site of fully oxidized cytochrome c oxidase could suppress the proton pump.
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PDB codes: 2zxw 3abl 3abm
19015819 J.Kulys, Z.Dapkunas, and R.Stupak (2009).
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19264758 K.Marjamaa, E.M.Kukkola, and K.V.Fagerstedt (2009).
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19099078 L.Fruk, J.Kuhlmann, and C.M.Niemeyer (2009).
Analysis of heme-reconstitution of apoenzymes by means of surface plasmon resonance.
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20009336 L.Qiang, and J.Zhou (2009).
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  Anal Sci, 25, 1467-1470.  
19240329 R.L.Owen, A.R.Pearson, A.Meents, P.Boehler, V.Thominet, and C.Schulze-Briese (2009).
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17446401 G.Katona, P.Carpentier, V.Nivière, P.Amara, V.Adam, J.Ohana, N.Tsanov, and D.Bourgeois (2007).
Raman-assisted crystallography reveals end-on peroxide intermediates in a nonheme iron enzyme.
  Science, 316, 449-453.
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17565988 H.P.Hersleth, T.Uchida, A.K.Røhr, T.Teschner, V.Schünemann, T.Kitagawa, A.X.Trautwein, C.H.Görbitz, and K.K.Andersson (2007).
Crystallographic and spectroscopic studies of peroxide-derived myoglobin compound II and occurrence of protonated FeIV O.
  J Biol Chem, 282, 23372-23386.
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  18379640 I.G.Denisov, D.C.Victoria, and S.G.Sligar (2007).
Cryoradiolytic reduction of heme proteins: Maximizing dose dependent yield.
  Radiat Phys Chem Oxf Engl 1993, 76, 714-721.  
17190816 K.Kühnel, E.Derat, J.Terner, S.Shaik, and I.Schlichting (2007).
Structure and quantum chemical characterization of chloroperoxidase compound 0, a common reaction intermediate of diverse heme enzymes.
  Proc Natl Acad Sci U S A, 104, 99.
PDB code: 2j5m
17303078 L.Huang, and P.R.Ortiz de Montellano (2007).
Arthromyces ramosus peroxidase produces two chlorinating species.
  Biochem Biophys Res Commun, 355, 581-586.  
17657769 L.M.Colosi, Q.Huang, and W.J.Weber (2007).
Validation of a two-parameter quantitative structure-activity relationship as a legitimate tool for rational re-design of horseradish peroxidase.
  Biotechnol Bioeng, 98, 295-299.  
17318598 M.A.Carrondo, I.Bento, P.M.Matias, and P.F.Lindley (2007).
Crystallographic evidence for dioxygen interactions with iron proteins.
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17704563 M.C.Corbett, M.J.Latimer, T.L.Poulos, I.F.Sevrioukova, K.O.Hodgson, and B.Hedman (2007).
Photoreduction of the active site of the metalloprotein putidaredoxin by synchrotron radiation.
  Acta Crystallogr D Biol Crystallogr, 63, 951-960.  
17114227 N.Mogharrab, H.Ghourchian, and M.Amininasab (2007).
Structural stabilization and functional improvement of horseradish peroxidase upon modification of accessible lysines: experiments and simulation.
  Biophys J, 92, 1192-1203.  
17229156 P.Ascenzi, A.Bocedi, G.Antonini, M.Bolognesi, and M.Fasano (2007).
Reductive nitrosylation and peroxynitrite-mediated oxidation of heme-hemopexin.
  FEBS J, 274, 551-562.  
17507985 P.F.Widboom, E.N.Fielding, Y.Liu, and S.D.Bruner (2007).
Structural basis for cofactor-independent dioxygenation in vancomycin biosynthesis.
  Nature, 447, 342-345.
PDB code: 2np9
18021062 P.Nicholls (2007).
The oxygenase-peroxidase theory of Bach and Chodat and its modern equivalents: change and permanence in scientific thinking as shown by our understanding of the roles of water, peroxide, and oxygen in the functioning of redox enzymes.
  Biochemistry (Mosc), 72, 1039-1046.  
18021063 P.R.Rich, and M.Iwaki (2007).
A comparison of catalytic site intermediates of cytochrome c oxidase and peroxidases.
  Biochemistry (Mosc), 72, 1047-1055.  
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.  
17403665 S.Ichimura, T.Uchida, S.Taniguchi, S.Hira, T.Tosha, I.Morishima, T.Kitagawa, and K.Ishimori (2007).
Unique peroxidase reaction mechanism in prostaglandin endoperoxide H synthase-2: compound I in prostaglandin endoperoxide H synthase-2 can be formed without assistance by distal glutamine residue.
  J Biol Chem, 282, 16681-16690.  
17881827 V.de 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
17328023 Z.H.Wang, Y.W.Lin, F.I.Rosell, F.Y.Ni, H.J.Lu, P.Y.Yang, X.S.Tan, X.Y.Li, Z.X.Huang, and A.G.Mauk (2007).
Converting cytochrome C into a peroxidase-like metalloenzyme by molecular design.
  Chembiochem, 8, 607-609.  
16843891 B.Kauffmann, M.S.Weiss, V.S.Lamzin, and A.Schmidt (2006).
How to avoid premature decay of your macromolecular crystal: a quick soak for long life.
  Structure, 14, 1099-1105.  
16698776 B.U.Klink, R.S.Goody, and A.J.Scheidig (2006).
A newly designed microspectrofluorometer for kinetic studies on protein crystals in combination with x-ray diffraction.
  Biophys J, 91, 981-992.
PDB codes: 2ce2 2ce5 2cf1 2cl0 2cl6 2cl7 2clc 2cld 2evw
16369092 E.F.Garman, and R.L.Owen (2006).
Cryocooling and radiation damage in macromolecular crystallography.
  Acta Crystallogr D Biol Crystallogr, 62, 32-47.  
16791642 G.Battistuzzi, M.Bellei, F.De Rienzo, and M.Sola (2006).
Redox properties of the Fe3+/Fe2+ couple in Arthromyces ramosus class II peroxidase and its cyanide adduct.
  J Biol Inorg Chem, 11, 586-592.  
16688708 G.Zoppellaro, T.Teschner, E.Harbitz, V.Schünemann, S.Karlsen, D.M.Arciero, S.Ciurli, A.X.Trautwein, A.B.Hooper, and K.K.Andersson (2006).
Low-temperature EPR and Mössbauer spectroscopy of two cytochromes with His-Met axial coordination exhibiting HALS signals.
  Chemphyschem, 7, 1258-1267.  
16421442 H.K.Leiros, J.Timmins, R.B.Ravelli, and S.M.McSweeney (2006).
Is radiation damage dependent on the dose rate used during macromolecular crystallography data collection?
  Acta Crystallogr D Biol Crystallogr, 62, 125-132.
PDB codes: 2bxy 2bxz 2by0 2by1 2by2 2by3 2by5 2by6 2by7 2by8 2by9 2bya
16738731 J.C.Thomas, C.Pacholski, and M.J.Sailor (2006).
Delivery of nanogram payloads using magnetic porous silicon microcarriers.
  Lab Chip, 6, 782-787.  
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.  
16895990 K.L.Stone, R.K.Behan, and M.T.Green (2006).
Resonance Raman spectroscopy of chloroperoxidase compound II provides direct evidence for the existence of an iron(IV)-hydroxide.
  Proc Natl Acad Sci U S A, 103, 12307-12310.  
16832798 L.Fruk, J.Müller, and C.M.Niemeyer (2006).
Kinetic analysis of semisynthetic peroxidase enzymes containing a covalent DNA-heme adduct as the cofactor.
  Chemistry, 12, 7448-7457.  
16352605 M.Grabolle, M.Haumann, C.Müller, P.Liebisch, and H.Dau (2006).
Rapid loss of structural motifs in the manganese complex of oxygenic photosynthesis by X-ray irradiation at 10-300 K.
  J Biol Chem, 281, 4580-4588.  
16762924 S.K.Badyal, M.G.Joyce, K.H.Sharp, H.E.Seward, M.Mewies, J.Basran, I.K.Macdonald, P.C.Moody, and E.L.Raven (2006).
Conformational mobility in the active site of a heme peroxidase.
  J Biol Chem, 281, 24512-24520.
PDB codes: 2ggn 2ghc 2ghd 2ghe 2ghh 2ghk
16470900 S.P.de Visser (2006).
Differences in and comparison of the catalytic properties of heme and non-heme enzymes with a central oxo-iron group.
  Angew Chem Int Ed Engl, 45, 1790-1793.  
16633684 T.Prieto, R.O.Marcon, F.M.Prado, A.C.Caires, P.Di Mascio, S.Brochsztain, O.R.Nascimento, and I.L.Nantes (2006).
Reaction route control by microperoxidase-9/CTAB micelle ratios.
  Phys Chem Chem Phys, 8, 1963-1973.  
16855866 W.Wu, J.Lu, Y.Wei, J.Wang, J.Lin, S.Cao, X.Sun, and K.Tang (2006).
Isolation and characterization of the first putative peroxidase gene from oilseed rape (Brassica napus) which is highly homologous to HRPC.
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16512409 X.Yan, X.Shi, K.Hill, and H.F.Ji (2006).
Microcantilevers modified by horseradish peroxidase intercalated nano-assembly for hydrogen peroxide detection.
  Anal Sci, 22, 205-208.  
15883191 A.P.Dubnovitsky, R.B.Ravelli, A.N.Popov, and A.C.Papageorgiou (2005).
Strain relief at the active site of phosphoserine aminotransferase induced by radiation damage.
  Protein Sci, 14, 1498-1507.
PDB codes: 2bhx 2bi1 2bi2 2bi3 2bi5 2bi9 2bia 2bie 2big
16041079 A.Schmidt, and V.S.Lamzin (2005).
Extraction of functional motion in trypsin crystal structures.
  Acta Crystallogr D Biol Crystallogr, 61, 1132-1139.
PDB codes: 1xvm 1xvo
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.  
16110518 C.Rovira (2005).
Structure, protonation state and dynamics of catalase compound II.
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16129597 D.Bourgeois, and A.Royant (2005).
Advances in kinetic protein crystallography.
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15723206 D.Kumar, S.P.de Visser, P.K.Sharma, E.Derat, and S.Shaik (2005).
The intrinsic axial ligand effect on propene oxidation by horseradish peroxidase versus cytochrome P450 enzymes.
  J Biol Inorg Chem, 10, 181-189.  
15899697 L.G.Fenoll, F.García-Molina, M.A.Gilabert, R.Varón, P.A.García-Ruiz, J.Tudela, F.García-Cánovas, and J.N.Rodríguez-López (2005).
Interpretation of the reactivity of peroxidase compound II with phenols and anilines using the Marcus equation.
  Biol Chem, 386, 351-360.  
16221678 M.Shintaku, K.Matsuura, S.Yoshioka, S.Takahashi, K.Ishimori, and I.Morishima (2005).
Absence of a detectable intermediate in the compound I formation of horseradish peroxidase at ambient temperature.
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15817398 O.Carugo, and K.Djinović Carugo (2005).
When X-rays modify the protein structure: radiation damage at work.
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16234928 R.Silaghi-Dumitrescu, and C.E.Cooper (2005).
Transient species involved in catalytic dioxygen/peroxide activation by hemoproteins: possible involvement of protonated Compound I species.
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16211084 X.Carpena, B.Wiseman, T.Deemagarn, R.Singh, J.Switala, A.Ivancich, I.Fita, and P.C.Loewen (2005).
A molecular switch and electronic circuit modulate catalase activity in catalase-peroxidases.
  EMBO Rep, 6, 1156-1162.
PDB codes: 2b2o 2b2q 2b2r 2b2s 5sw4 5sw5 5sw6 5sx0
16155883 Y.K.Choe, and S.Nagase (2005).
Effect of the axial cysteine ligand on the electronic structure and reactivity of high-valent iron(IV) oxo-porphyrins (Compound I): a theoretical study.
  J Comput Chem, 26, 1600-1611.  
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
15333928 J.Wang, and S.E.Ealick (2004).
Observation of time-resolved structural changes by linear interpolation of highly redundant X-ray diffraction data.
  Acta Crystallogr D Biol Crystallogr, 60, 1579-1585.  
15173586 J.Wuerges, J.W.Lee, Y.I.Yim, H.S.Yim, S.O.Kang, and K.Djinovic Carugo (2004).
Crystal structure of nickel-containing superoxide dismutase reveals another type of active site.
  Proc Natl Acad Sci U S A, 101, 8569-8574.
PDB codes: 1q0d 1q0f 1q0g 1q0k 1q0m
15339813 K.Nilsson, H.P.Hersleth, T.H.Rod, K.K.Andersson, and U.Ryde (2004).
The protonation status of compound II in myoglobin, studied by a combination of experimental data and quantum chemical calculations: quantum refinement.
  Biophys J, 87, 3437-3447.  
15653431 M.A.Gilabert, L.G.Fenoll, F.García-Molina, P.A.García-Ruiz, J.Tudela, F.García-Cánovas, and J.N.Rodríguez-López (2004).
Stereospecificity of horseradish peroxidase.
  Biol Chem, 385, 1177-1184.  
15159561 M.Schiltz, P.Dumas, E.Ennifar, C.Flensburg, W.Paciorek, C.Vonrhein, and G.Bricogne (2004).
Phasing in the presence of severe site-specific radiation damage through dose-dependent modelling of heavy atoms.
  Acta Crystallogr D Biol Crystallogr, 60, 1024-1031.  
15192224 M.T.Green, J.H.Dawson, and H.B.Gray (2004).
Oxoiron(IV) in chloroperoxidase compound II is basic: implications for P450 chemistry.
  Science, 304, 1653-1656.  
14966119 M.Unno, T.Matsui, G.C.Chu, M.Couture, T.Yoshida, D.L.Rousseau, J.S.Olson, and M.Ikeda-Saito (2004).
Crystal structure of the dioxygen-bound heme oxygenase from Corynebacterium diphtheriae: implications for heme oxygenase function.
  J Biol Chem, 279, 21055-21061.
PDB code: 1v8x
15026418 R.Kort, K.J.Hellingwerf, and R.B.Ravelli (2004).
Initial events in the photocycle of photoactive yellow protein.
  J Biol Chem, 279, 26417-26424.
PDB codes: 1uwn 1uwp
15341736 V.Adam, A.Royant, V.Nivière, F.P.Molina-Heredia, and D.Bourgeois (2004).
Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray-induced photo-reduction.
  Structure, 12, 1729-1740.
PDB codes: 1vzg 1vzh 1vzi
12750363 I.Bento, V.H.Teixeira, A.M.Baptista, C.M.Soares, P.M.Matias, and M.A.Carrondo (2003).
Redox-Bohr and other cooperativity effects in the nine-heme cytochrome C from Desulfovibrio desulfuricans ATCC 27774: crystallographic and modeling studies.
  J Biol Chem, 278, 36455-36469.
PDB codes: 1ofw 1ofy
12777808 K.Diederichs, S.McSweeney, and R.B.Ravelli (2003).
Zero-dose extrapolation as part of macromolecular synchrotron data reduction.
  Acta Crystallogr D Biol Crystallogr, 59, 903-909.  
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
12609902 M.Tanaka, K.Matsuura, S.Yoshioka, S.Takahashi, K.Ishimori, H.Hori, and I.Morishima (2003).
Activation of hydrogen peroxide in horseradish peroxidase occurs within approximately 200 micro s observed by a new freeze-quench device.
  Biophys J, 84, 1998-2004.  
12668455 R.Fedorov, I.Schlichting, E.Hartmann, T.Domratcheva, M.Fuhrmann, and P.Hegemann (2003).
Crystal structures and molecular mechanism of a light-induced signaling switch: The Phot-LOV1 domain from Chlamydomonas reinhardtii.
  Biophys J, 84, 2474-2482.
PDB codes: 1n9l 1n9n 1n9o
12944259 R.R.Gabdoulline, U.Kummer, L.F.Olsen, and R.C.Wade (2003).
Concerted simulations reveal how peroxidase compound III formation results in cellular oscillations.
  Biophys J, 85, 1421-1428.  
12215454 I.G.Denisov, T.M.Makris, and S.G.Sligar (2002).
Formation and decay of hydroperoxo-ferric heme complex in horseradish peroxidase studied by cryoradiolysis.
  J Biol Chem, 277, 42706-42710.  
12351824 K.Meno, S.Jennings, A.T.Smith, A.Henriksen, and M.Gajhede (2002).
Structural analysis of the two horseradish peroxidase catalytic residue variants H42E and R38S/H42E: implications for the catalytic cycle.
  Acta Crystallogr D Biol Crystallogr, 58, 1803-1812.
PDB codes: 1kzm 4atj
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.

 

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