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- W2169324935 abstract "A cobalt-porphyrin containing protein has been isolated from the sulfate-reducer Desulfovibrio desulfuricans (Norway). This violet-colored protein has a molecular weight of approx. 13,000 daltons and contains 1 cobalt atom/molecule. The apo-protein was estimated to contain 104 amino-acid residues giving a molecular weight of 11,000 daltons. The UV-visible absorption spectrum of the protein exhibiting maxima at 588,418 and 280 nm with a shoulder at 550 nm is characteristic of metalloporphyrin proteins. The molar extinction coefficients of the cobalt-protein at 588, 418 and 280 nm are 31,330 , 64,670 and 17,200 respectively and its absorbance ratio A280A588 is 0.54. The protein is reduced by dithionite giving a blue-colored reduced form. Important spectral modifications of the chromophore occurred during the reduction including a shift of the Soret peak from 418 to 381 nm and a shift of the α band in the opposite direction from 588 to 593.5 nm. The Co-protein was slowly reduced by the hydrogenase from D.desulfuricans under hydrogen in the presence of cytochrome C3. The reported data suggest that the redox states of the cobalt center of this new electron carrier correspond to the Co(III) and Co(II) states." @default.
- W2169324935 created "2016-06-24" @default.
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- W2169324935 date "1981-11-01" @default.
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- W2169324935 title "A cobalt porphyrin containing protein reducible by hydrogenase isolated from Desulfovibrio desulfuricans (Norway)" @default.
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- W2169324935 doi "https://doi.org/10.1016/0006-291x(81)90483-6" @default.
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