Title : Crystal structure and characterization of a cytochrome c peroxidase-cytochrome c site-specific cross-link.

Pub. Date : 2004 Apr 20

PMID : 15071191






2 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 c) has been made by engineering cysteines into CCP and cyt. Cysteine cytochrome-c peroxidase Saccharomyces cerevisiae S288C
2 UV-visible spectroscopic and stopped-flow studies indicate that CCP in the covalent complex reacts normally with H(2)O(2) to give compound I. Stopped-flow kinetic studies also show that intramolecular electron transfer between the cross-linked ferrocytochrome c and the Trp-191 cation radical site in CCP compound I occurs fast and is nearly complete within the dead time ( approximately 2 ms) of the instrument. Tryptophan cytochrome-c peroxidase Saccharomyces cerevisiae S288C