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A EcDos
H 2 O(OH - )
Met95
CO
Fe 2+
Fe 2+
Fe 3+
His7 7
His77
His77
B GSU0582/0935 and DcrA
H 2 O(OH - )
X (Met?)
CO
Fe 3+
Fe 2+
Fe 2+
His
Figure 7.12 Coordination structures of the haem in (A) GSU0582/GSU0953 and
(B) EcDos.
n 2 and n 3 bands at 1567/1588 cm 1 and 1483/1508 cm 1 for GSU0582
and at 1570/1590 cm 1 and 1479/1508 cm 1 for GSU0935, respectively
( Catarino et al., 2010 ), which indicate that the ferric haem is in a mixture
of a 6-coordinate and low-spin and a 6-coordinate and high-spin states.
Though the ferrous haem in GSU0582 and GSU0935 is 6-coordinated, it
can bind CO and NO to form the CO- and NO-bound haems as are the cases
of Ec Dos, CooA, and DcrA. Formation of a stable O 2 -bound form is not
reported for GSU0582 and GSU0935. Resonance Raman spectroscopy
reveals formation of a mixture of a 6-coordinate and low-spin nitrosyl haem,
and a 5-coordinate and high-spin nitrosyl haem upon the reaction of ferrous
GSU0582 or GSU0935 with NO ( Catarino et al., 2010 ). Upon the reaction
of ferric GSU0582 and GSU0935 with NO, a 6-coordinate Fe 3 þ -nitrosyl
haem is formed along with a 5-coordinate Fe 2 þ -nitrosyl haem produced
by reductive nitrosylation ( Catarino et al., 2010 ). The K d values of
GSU0582 and GSU0935 for CO to the ferrous haem, NO to the ferrous
haem, and NO to the ferric haem are 0.05, 0.08, and 0.34 m M, and 0.08,
0.04, and 17 m M, respectively. MD calculations reveal that the difference
of K d (NO) for the ferric haems between GSU0582 and GSU0935 can be rat-
ionalised in terms of distal haem pocket accessibility ( Catarino et al., 2010 ).
6.3.2 DcrA
The amino acid sequence of DcrA from Desulfovibrio vulgaris Hildenborough
indicates homology with the methyl-accepting chemotaxis proteins from
enteric bacteria ( Deckers & Voordouw, 1996; Dolla, Fu, Brumlik, &
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