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Rapid intrachain binding of histidine-26 and histidine-33 to heme in unfolded ferrocytochrome C.

Abstract：

:Time-resolved spectroscopic studies of unfolded horse iron(II) cytochrome c have suggested that the imidazole side chains of His26 and His33 bind transiently to the heme iron on microsecond time scales, after photodissociation of a carbon monoxide ligand from the heme. Our studies of four variants of cytochrome c (horse wild type, horse H33N, horse H33N/H26Q, and tuna wild type), unfolded in guanidine hydrochloride at pH 6.5, demonstrate that these side chains are responsible for the observed microsecond spectral changes. As His33 and then His26 are eliminated from the horse wild-type sequence, transient optical absorption spectra show systematic suppression of a rapid (approximately 10-100 micros) Soret absorbance change that follows photolysis of CO. Transient binding of these histidine side chains to the heme therefore generates one of the fast kinetic phases observed in previous photochemically triggered spectroscopic studies of dynamics in unfolded iron(II) cytochrome c. Furthermore, both His33 and His26 appear to contribute to a similar extent in these early kinetics. Thus, the stiffness of the polypeptide chain creates a deviation from Gaussian chain behavior by impeding, although not preventing, the formation of short (<10 peptide bonds) intrachain loops around the heme group.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Hagen SJ,Latypov RF,Dolgikh DA,Roder H

doi

10.1021/bi011371a

subject

Has Abstract

pub_date

2002-01-29 00:00:00

pages

1372-80

issue

4

eissn

0006-2960

issn

1520-4995

pii

bi011371a

journal_volume

41

pub_type

杂志文章

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