Abstract:
:The primary electron acceptor complex of photosystem II, QAFe2+, can bind a number of small molecules at the iron site, including cyanide [Koulougliotis, D., Kostopoulos, T., Petrouleas, V., & Diner, B. A. (1993) Biochim. Biophys. Acta 1141, 275-282)]. In the presence of NaCN (30-300 mM) at pH 6.5, the reduced state, QA-Fe2+, produced either by illumination at < or = 200 K or by reduction in the dark with sodium dithionite, is characterized by a g = 1.98 EPR signal. The light- or dithionite-induced g = 1.98 signal decays with increasing pH above 6.5 and is almost totally absent at pH 8.1 and NaCN concentrations above 300 mM. However, at high pH (8.1), the g = 1.98 signal still forms transiently before it decays with a t1/2 of approximately 30 min in spinach BBY preparations treated with 100 mM NaCN. Complementary to the disappearance of the g = 1.98 signal with increasing pH or incubation time, a new EPR signal develops at g = 2.0045. This signal has the characteristics of the semiquinone, QA-, uncoupled from its magnetic interaction with the iron. Prolonged incubation of a high pH, high cyanide treated sample in a cyanide-free medium at pH 6 restores the ability of the sample to develop the cyanide-induced g = 1.98 signal at pH 6.5. This indicates that the iron is not physically dissociated during the high pH cyanide treatment. The high pH, high cyanide effects are accompanied by the conversion of the characteristic Fe2+ (S = 2) Mössbauer doublet [isomer shift (Fe) = 1.19 mm/s, quadrupole splitting = 2.95 mm/s] to a new one with parameters (isomer shift = 0.26 mm/s, quadrupole splitting = 0.36 mm/s) characteristic of an Fe2+(S = 0) state.(ABSTRACT TRUNCATED AT 250 WORDS)
journal_name
Biochemistryjournal_title
Biochemistryauthors
Sanakis Y,Petrouleas V,Diner BAdoi
10.1021/bi00199a014subject
Has Abstractpub_date
1994-08-23 00:00:00pages
9922-8issue
33eissn
0006-2960issn
1520-4995journal_volume
33pub_type
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