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2.2 A structure of oxy-peroxidase as a model for the transient enzyme: peroxide complex.

Miller MA, Shaw A, Kraut J
Nat Struct Biol 1 524-31 (1994)
Cited: 19 times
EuropePMC logo PMID: 7664080

Abstract

The Fe+3-OOH complex of peroxidases has a very short half life, and its structure cannot be determined by conventional methods. The Fe+2-O2 complex provides a useful structural model for this intermediate, as it differs by only one electron and one proton from the transient Fe+3-OOH complex. We therefore determined the crystal structure of the Fe+2-O2 complex formed by a yeast cytochrome c peroxidase mutant with Trp 191 replaced by Phe. The refined structure shows that dioxygen can form a hydrogen bond with the conserved distal His residue, but not with the conserved distal Arg residue. When the transient Fe+3-OOH complex is modelled in a similar orientation, the active site of peroxidase appears to be optimized for catalysing proton transfer between the vicinal oxygen atoms of the peroxy-anion.

Reviews - 1dcc mentioned but not cited (1)

  1. Specificity and selectivity in post-translational biotin addition. Beckett D. Biochem Soc Trans 46 1577-1591 (2018)


Reviews citing this publication (6)

  1. Insight into protein structure and protein-ligand recognition by Fourier transform infrared spectroscopy. Jung C. J Mol Recognit 13 325-351 (2000)
  2. Mechanisms of compound I formation in heme peroxidases. Hiner AN, Raven EL, Thorneley RN, García-Cánovas F, Rodríguez-López JN. J Inorg Biochem 91 27-34 (2002)
  3. Understanding heme cavity structure of peroxidases: comparison of electronic absorption and resonance Raman spectra with crystallographic results. Smulevich G. Biospectroscopy 4 S3-17 (1998)
  4. Spectroscopic studies of the cytochrome P450 reaction mechanisms. Mak PJ, Denisov IG. Biochim Biophys Acta Proteins Proteom 1866 178-204 (2018)
  5. Cytochrome c oxidase as a proton-pumping peroxidase: reaction cycle and electrogenic mechanism. Konstantinov AA. J Bioenerg Biomembr 30 121-130 (1998)
  6. Crystallographic evidence for dioxygen interactions with iron proteins. Carrondo MA, Bento I, Matias PM, Lindley PF. J Biol Inorg Chem 12 429-442 (2007)

Articles citing this publication (12)

  1. Role of arginine 38 in horseradish peroxidase. A critical residue for substrate binding and catalysis. Rodriguez-Lopez JN, Smith AT, Thorneley RN. J Biol Chem 271 4023-4030 (1996)
  2. Resonance Raman spectroscopy of oxoiron(IV) porphyrin pi-cation radical and oxoiron(IV) hemes in peroxidase intermediates. Terner J, Palaniappan V, Gold A, Weiss R, Fitzgerald MM, Sullivan AM, Hosten CM. J Inorg Biochem 100 480-501 (2006)
  3. The mechanism of Compound I formation revisited. Jones P, Dunford HB. J Inorg Biochem 99 2292-2298 (2005)
  4. Characterization of Class III Peroxidases from Switchgrass. Moural TW, Lewis KM, Barnaba C, Zhu F, Palmer NA, Sarath G, Scully ED, Jones JP, Sattler SE, Kang C. Plant Physiol 173 417-433 (2017)
  5. Protein conformer selection by ligand binding observed with crystallography. Cao Y, Musah RA, Wilcox SK, Goodin DB, McRee DE. Protein Sci 7 72-78 (1998)
  6. Role of the oxyferrous heme intermediate and distal side adduct radical in the catalase activity of Mycobacterium tuberculosis KatG revealed by the W107F mutant. Zhao X, Yu S, Ranguelova K, Suarez J, Metlitsky L, Schelvis JP, Magliozzo RS. J Biol Chem 284 7030-7037 (2009)
  7. Role of histidine 42 in ascorbate peroxidase. Kinetic analysis of the H42A and H42E variants. Lad L, Mewies M, Basran J, Scrutton NS, Raven EL. Eur J Biochem 269 3182-3192 (2002)
  8. Charge reversal of a critical active-site residue of cytochrome-c peroxidase: characterization of the Arg48-->Glu variant. Bujons J, Dikiy A, Ferrer JC, Banci L, Mauk AG. Eur J Biochem 243 72-84 (1997)
  9. Hydrogen-bonding conformations of tyrosine B10 tailor the hemeprotein reactivity of ferryl species. De Jesús-Bonilla W, Cruz A, Lewis A, Cerda J, Bacelo DE, Cadilla CL, López-Garriga J. J Biol Inorg Chem 11 334-342 (2006)
  10. Absorption into fluorescence. A method to sense biologically relevant gas molecules. Strianese M, Varriale A, Staiano M, Pellecchia C, D'Auria S. Nanoscale 3 298-302 (2011)
  11. Interaction with the Redox Cofactor MYW and Functional Role of a Mobile Arginine in Eukaryotic Catalase-Peroxidase. Gasselhuber B, Graf MM, Jakopitsch C, Zamocky M, Nicolussi A, Furtmüller PG, Oostenbrink C, Carpena X, Obinger C. Biochemistry 55 3528-3541 (2016)
  12. Biomimic O2 activation hydroxylates a meso-carbon of the porphyrin ring regioselectively under mild conditions. Yamanishi K, Yairi T, Suzuki K, Kondo M. Chem Commun (Camb) 49 9296-9298 (2013)


Related citations provided by authors (3)

  1. Reaction of Ferrous Cytochrome C Peroxidase with Dioxygen: Site-Directed Mutagenesis Provides Evidence for Rapid Reduction of Dioxygen by Intramolecular Electron Transfer from the Compound I Radical Site. Miller MA, Bandyopadhyay D, Mauro JM, Taylor TG, Kraut J Biochemistry 31 2789- (1992)
  2. X-Ray Structures of Recombinant Yeast Cytochrome C Peroxidase and Three Heme Cleft Mutants Prepared by Site-Directed Mutagenesis. Wang J, Mauro JM, Edwards SL, Oatley SJ, Fishel LA, Ashford VA, Xuong N-H, Kraut J Biochemistry 29 7160- (1990)
  3. Crystal Structure of Yeast Cytochrome C Peroxidase Refined at 1.7 Angstroms Resolution. Finzel BC, Poulos TL, Kraut J J. Biol. Chem. 259 13027- (1984)

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