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. Author manuscript; available in PMC: 2009 Jul 1.
Published in final edited form as: Biochim Biophys Acta. 2008 May 1;1777(7-8):1001–1019. doi: 10.1016/j.bbabio.2008.04.037

Table 4.

Kinetic characteristics of strains with Asn-221 of cytochrome b modified
Strain Photosynthetic growth Reduction of bHa Fraction of bH reduced b Em,7, pH dependence d Reoxid. (t½/ms) e
cyt b150 bH, no inhib. with AA
Wild type +++ 455 0.05 148, −59 32, −59 46, 0 <1.6
N221D +++ (as wt) 0.8 150 −59 35, −54 −47, −59 15
N221H +++ 520 0.68 150, −59 35, −59 13, −50 12
N221P +++ 442 0.167 154, −59 38, −59 −3, −59 2.0
N221T +++ (as wt) 0.37 140, −59 29, −50 13, 59 8.0
N221I +++ (as wt) 0.75 104, −59 36, −59 −95, −59 14
a

Notes: Rate of reduction of heme bH measured following a 5 µs flash at Eh ~120 mV in the presence of antimycin (units – mol cyt bH /mol bc1 complex / sec).

b

Fraction of heme bH reduced at the maximal amplitude (at ~3–5 ms) of the kinetic trace in the absence of antimycin, compared to the fraction reduced in the presence of antimycin.

c

Rate of reoxidation of heme bH in the absence of antimycin, measured by subtraction of the traces in the presence and absence of antimycin (units – mol cyt bH /mol bc1 complex / sec). The rate in the wild-type reflects the rate-limiting reduction of the low potential chain through the Qo-site reaction. Since v = k(occupancy), and the fraction of heme bH in the reduced form (column 4) is <<1, the rate constant must be much greater than that for the limiting step.

d

Em,7 in mV, pH dependence of Em in mV/pH unit, assuming a single component for each heme.

e

Half-times for reoxidation of heme bH measured from kinetic traces.