A comparative flash-photolysis study of electron transfer from pea and spinach plastocyanins to spinach Photosystem 1. A reaction involving a rate-limiting conformational change

1996 ◽  
Vol 50 (1) ◽  
pp. 11-21 ◽  
Author(s):  
Kalle Sigfridsson ◽  
Shiping He ◽  
Sandeep Modi ◽  
Derek S. Bendall ◽  
John Gray ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Conformational Change ◽  
Flash Photolysis ◽  
Photosystem 1 ◽  
Rate Limiting

Electron transfer sensitized photolysis of 'onium salts

1988 ◽  
Vol 66 (2) ◽  
pp. 319-324 ◽  
Author(s):  
R. J. DeVoe ◽  
M. R. V. Sahyun ◽  
Einhard Schmidt ◽  
N. Serpone ◽  
D. K. Sharma
Keyword(s):  
Electron Transfer ◽  
Flash Photolysis ◽  
Laser Flash Photolysis ◽  
Laser Flash ◽  
Quantitative Model ◽  
Intersystem Crossing ◽  
Single Electron Transfer ◽  
Onium Salts ◽  
Encounter Complex ◽  
Back Electron Transfer

We have studied the anthracene-sensitized photolyses of both diphenyliodonium and triphenylsulphonium salts in solution using both steady-state and laser flash photolysis techniques. Photoproducts, namely, phenylated anthracenes along with iodobenzene or diphenylsulphide, respectively, are obtained from both salts with quantum efficiencies of ca. 0.1 at 375 nm. We infer the intermediacy of diphenyliodo and triphenylsulphur radicals formed by single electron transfer from the singlet-excited anthracene. We have developed a quantitative model of this chemistry, and identify the principal sources of inefficiency as back electron transfer, which occurs at nearly the theoretically limiting rate, intersystem crossing from the initially formed sensitizer–'onium salt encounter complex, and in-cage radical recombination.

Laser flash photolysis studies of intramolecular electron transfer in milk xanthine oxidase

Biochemistry ◽  
1983 ◽  
Vol 22 (23) ◽  
pp. 5270-5279 ◽  
Author(s):  
Anjan Bhattacharyya ◽  
Gordon Tollin ◽  
Michael Davis ◽  
Dale E. Edmondson
Keyword(s):  
Electron Transfer ◽  
Xanthine Oxidase ◽  
Flash Photolysis ◽  
Laser Flash Photolysis ◽  
Laser Flash ◽  
Intramolecular Electron Transfer

scholarly journals A stopped-flow kinetic study of soluble methane mono-oxygenase from Methylococcus capsulatus (Bath)

1989 ◽  
Vol 259 (1) ◽  
pp. 167-172 ◽  
Author(s):  
J Green ◽  
H Dalton
Keyword(s):  
Electron Transfer ◽  
Protein C ◽  
Turnover Rate ◽  
Protein A ◽  
Methylococcus Capsulatus ◽  
Bond Breakage ◽  
Conversion Of Methane ◽  
Protein Components ◽  
A Charge ◽  
Rate Limiting

1. The roles of the three protein components of soluble methane mono-oxygenase were investigated by the use of rapid-reaction techniques. The transfer of electrons through the enzyme complex from NADH to methane/O2 was also investigated. 2. Electron transfer from protein C, the reductase component, to protein A, the hydroxylase component, was demonstrated. Protein C was shown to undergo a three-electron--one-electron catalytic cycle. The interaction of protein C with NADH was investigated. Reduction of protein C was shown to be rapid, and a charge-transfer interaction between reduced FAD and NAD+ was observed; this intermediate was also found in static titration experiments. Thus the binding of NADH, the reduction of protein C and the intramolecular transfer of electrons through protein C were shown to be much more rapid than the turnover rate of methane mono-oxygenase. 3. The rate of transfer of electrons from protein C to protein A was shown to be lower than the reduction of protein C but higher than the turnover rate of methane mono-oxygenase. Association of the proteins was not rate-limiting. The amount of protein A present in the system had a small effect on the rate of reduction of protein C, indicating some co-operativity between the two proteins. 4. Protein B was shown to prevent electron transfer between protein C and protein A in the absence of methane. On addition of saturating concentrations of methane electron transfer was restored. With saturating concentrations of methane and O2 the observed rate constant for the conversion of methane into methanol was 0.26 s-1 at 18 degrees C. 5. By the use of [2H4]methane it was demonstrated that C-H-bond breakage is likely to be the rate-limiting step in the conversion of methane into methanol.

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