Plastocyanin

Pecht, Israel; Farver, Ole

doi:10.1002/047120918x.emb1144

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2006

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“…Cytochrome cd 1 from P. stutzeri strain ZoBell (ATCC 14405) was purified, and its biochemical and spectroscopic parameters were characterized as described (9). Pulse radiolysis experiments were performed on the Varian V-7715 linear accelerator of the Hebrew University in Jerusalem (10). Electrons accelerated to 5 MeV were used with pulse lengths in the range from 0.1 to 1.5 s and introduced into argon-saturated solutions containing 5 mM N-methylnicotinamide, 5 mM phosphate, 0.1 M tert-butanol, pH 7.0.…”

Section: Methodsmentioning

confidence: 99%

Allosteric control of internal electron transfer in cytochromecd 1 nitrite reductase

Farver

Kroneck

Pecht

et al. 2006

Rend. Fis. Acc. Lincei

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Cytochrome cd1 nitrite reductase is a bifunctional multiheme enzyme catalyzing the one-electron reduction of nitrite to nitric oxide and the four-electron reduction of dioxygen to water. Kinetics and thermodynamics of the internal electron transfer process in the Pseudomonas stutzeri enzyme have been studied and found to be dominated by pronounced interactions between the c and the d 1 hemes. The interactions are expressed both in dramatic changes in the internal electron-transfer rates between these sites and in marked cooperativity in their electron affinity. The results constitute a prime example of intraprotein control of the electrontransfer rates by allosteric interactions.

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Section: Methodsmentioning

confidence: 99%