Acta Crystallographica Section D
Acta Crystallographica
Section D
STRUCTURAL BIOLOGY
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Acta Cryst.
(2012).
D
68
,
144-153
https://doi.org/10.1107/S0907444911052632
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Covalent modifications of the catalytic tyrosine in octahaem cytochrome
c
nitrite reductase and their effect on the enzyme activity
A. A. Trofimov
,
K. M. Polyakov
,
T. V. Tikhonova
,
A. V. Tikhonov
,
T. N. Safonova
,
K. M. Boyko
,
P. V. Dorovatovskii
and
V. Popov
An unusual covalent bond between the side chains of the catalytic Tyr residue and Gln decreases the activity of cytochrome
c
nitrite reductase. The Tyr residue is a proton donor during the catalysis.
Keywords:
multihaem proteins
;
covalent bonds
;
proton transport
;
catalytic mechanism
.
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