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| High-resolution crystal structures and spectroscopy of native and compound I cytochrome c peroxidase |
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| Author(s): Bonagura CA, Bhaskar B, Shimizu H, Li HY, Sundaramoorthy M, McRee DE, Goodin DB, Poulos TL |
| Source: BIOCHEMISTRY Volume: 42 Issue: 19 Pages: 5600-5608 Published: MAY 20 2003 |
| Times Cited: 52 References: 44 |
| Abstract: Cytochrome c peroxidase (CCP) is a 32.5 kDa mitochondrial intermembrane space heme peroxidase from Saccharomyces cerevisiae that reduces H2O2 to 2H2O by oxidizing two molecules of cytochrome c (cyt c). Here we compare the 1.2 Angstrom native structure (CCP) with the 1.3 Angstrom 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 Angstrom suggesting a single Fe(IV)-O bond and not the generally accepted double bond. |
| Document Type: Article |
| Language: English |
| Reprint Address: Poulos, TL (reprint author), Univ Calif Irvine, Program macromol Struct, Dept Mol Biol & Biochem, Irvine, CA 92697 USA |
Addresses:
1. Univ Calif Irvine, Program macromol Struct, Dept Mol Biol & Biochem, Irvine, CA 92697 USA
2. Vanderbilt Univ, Med Ctr, Dept Med, Nashville, TN 37232 USA
3. Vanderbilt Univ, Med Ctr, Dept Nephrol, Nashville, TN 37232 USA
4. Vanderbilt Univ, Med Ctr, Dept Biochem, Nashville, TN 37232 USA
5. Syrrx Inc, San Diego, CA 92121 USA
6. Scripps Res Inst, La Jolla, CA 92037 USA |
| Publisher: AMER CHEMICAL SOC, 1155 16TH ST, NW, WASHINGTON, DC 20036 USA |
| Subject Category: Biochemistry & Molecular Biology |
| IDS Number: 679QW |
| ISSN: 0006-2960 |
| DOI: 10.1021/bi034058c |
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