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High-resolution crystal structures and spectroscopy of native and compound I cytochrome c peroxidase.

Bonagura CA, Bhaskar B, Shimizu H, Li H, Sundaramoorthy M, McRee DE, Goodin DB, Poulos TL
Biochemistry 42 5600-8 (2003)
Cited: 78 times
EuropePMC logo PMID: 12741816

Abstract

Cytochrome c peroxidase (CCP) is a 32.5 kDa mitochondrial intermembrane space heme peroxidase from Saccharomyces cerevisiae that reduces H(2)O(2) to 2H(2)O by oxidizing two molecules of cytochrome c (cyt c). Here we compare the 1.2 A native structure (CCP) with the 1.3 A structure of its stable oxidized reaction intermediate, Compound I (CCP1). In addition, crystals were analyzed by UV-vis absorption and electron paramagnetic resonance spectroscopies before and after data collection to determine the state of the Fe(IV) center and the cationic Trp191 radical formed in Compound I. The results show that X-ray exposure does not lead to reduction of Fe(IV) and only partial reduction of the Trp radical. A comparison of the two structures reveals subtle but important conformational changes that aid in the stabilization of the Trp191 cationic radical in Compound I. The higher-resolution data also enable a more accurate determination of changes in heme parameters. Most importantly, when one goes from resting state Fe(III) to Compound I, the His-Fe bond distance increases, the iron moves into the porphyrin plane leading to shorter pyrrole N-Fe bonds, and the Fe(IV)-O bond distance is 1.87 A, suggesting a single Fe(IV)-O bond and not the generally accepted double bond.

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  1. Heme enzyme structure and function. Poulos TL. Chem Rev 114 3919-3962 (2014)
  2. Oxygen Activation and Radical Transformations in Heme Proteins and Metalloporphyrins. Huang X, Groves JT. Chem Rev 118 2491-2553 (2018)
  3. On the status of ferryl protonation. Behan RK, Green MT. J Inorg Biochem 100 448-459 (2006)
  4. Structures of the high-valent metal-ion haem-oxygen intermediates in peroxidases, oxygenases and catalases. Hersleth HP, Ryde U, Rydberg P, Görbitz CH, Andersson KK. J Inorg Biochem 100 460-476 (2006)
  5. Thirty years of heme peroxidase structural biology. Poulos TL. Arch Biochem Biophys 500 3-12 (2010)
  6. Synthetic Fe/Cu Complexes: Toward Understanding Heme-Copper Oxidase Structure and Function. Adam SM, Wijeratne GB, Rogler PJ, Diaz DE, Quist DA, Liu JJ, Karlin KD. Chem Rev 118 10840-11022 (2018)
  7. A new look at the role of thiolate ligation in cytochrome P450. Yosca TH, Ledray AP, Ngo J, Green MT. J Biol Inorg Chem 22 209-220 (2017)
  8. The reaction mechanisms of heme catalases: an atomistic view by ab initio molecular dynamics. Alfonso-Prieto M, Vidossich P, Rovira C. Arch Biochem Biophys 525 121-130 (2012)
  9. The influence of X-rays on the structural studies of peroxide-derived myoglobin intermediates. Hersleth HP, Hsiao YW, Ryde U, Görbitz CH, Andersson KK. Chem Biodivers 5 2067-2089 (2008)

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