Intrinsic tryptophan phosphorescence as a marker of conformation and oxygen diffusion in purified cytochrome oxidase.

Abstract:

:Cytochrome oxidase exhibits phosphorescence from tryptophan in aqueous solution in the absence of oxygen. The lifetime for the resting reduced enzyme suspended in Tween-20 is around 30 ms at pH 8. The lifetime is longest between pH 7 and 8 and decreases with lowering of pH. Oxygen quenches the phosphorescence with a Stern-Volmer quenching constant of approximately 5 x 10(7) M-1.s-1 at 5 degrees C whereas cytochrome c has no effect. We interpret these results to indicate that room temperature tryptophan phosphorescence arises from tryptophan(s) in structured region(s) remote from the hemes and that the protein does not impose a significant barrier for the diffusion of oxygen.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Papp S,King TE,Vanderkooi JM

doi

10.1016/0014-5793(91)80566-l

keywords:

subject

Has Abstract

pub_date

1991-05-20 00:00:00

pages

113-6

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(91)80566-L

journal_volume

283

pub_type

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