Photodissociation of cytochrome oxidase-nitric oxide at low temperatures.

Abstract:

:Spectrophotometric studies revealed the irreversible photodissociation of reduced cytochrome oxidase-nitric oxide (NO) at 5 K. The dissociated NO recombined as the sample temperature was raised, and the half-recombination temperature was 65 K. The photodissociation at 5K was also confirmed by a change in the EPR spectrum; that is, ferroheme a-NO signals at gx=2.09 and gm=2.006 were replaced by a new signal at gm=2.03, and this change was reversed at the temperature of liquid nitrogen. Comparison of such behavior with that of cytochrome oxidase-carbon monoxide led us to propose that on photodissociation of NO from heme iron, the NO was trapped specifically at a site near the heme iron producing a new paramagnetic species. Its identification will require further studies.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Yoshida S,Hori H,Orii Y

doi

10.1093/oxfordjournals.jbchem.a133138

subject

Has Abstract

pub_date

1980-12-01 00:00:00

pages

1623-7

issue

6

eissn

0021-924X

issn

1756-2651

journal_volume

88

pub_type

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