EXAFS of the type-1 copper site of rusticyanin.

Abstract:

:Extended X-ray absorption fine structure (EXAFS) spectra at the Cu K-edge have been recorded of the oxidized and reduced form at pH 3.5 of rusticyanin, the type-1 or 'blue'-copper protein from Thiobacillus ferrooxidans. The EXAFS of oxidized rusticyanin is well simulated with models assuming a ligand set of 2 N(His) and 1 S(Cys) at 1.99 and 2.16 A, respectively. Upon reduction, the average Cu-N ligand distance increases by approx. 0.08A. For both redox states studied, the fit by the simulation is significantly improved by including a contribution of an additional sulfur ligand at approx. 2.8 A. From comparison with structural data of other blue-copper proteins, it is concluded that the copper coordination environment is relatively rigid, which may be a clue to its high redox potential.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Holt SD,Piggott B,Ingledew WJ,Feiters MC,Diakun GP

doi

10.1016/0014-5793(90)81133-9

subject

Has Abstract

pub_date

1990-08-20 00:00:00

pages

117-21

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(90)81133-9

journal_volume

269

pub_type

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