A resonance Raman study on the nature of charge‐transfer interactions in butyryl CoA dehydrogenase
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説明
Butyryl-CoA dehydrogenase (BCD) (EC 1.3.99.2) is a flavoprotein that catalyses the first step in fatty acid p-oxidation. When isolated from various sources, the pure enzyme has a characteristic green colour [l-3], due to a long-wavelength absorption band centred at 710 nm. We have proposed that a new chemical species, CoA persulphide, tightly-bound at the enzyme’s active site, is the donor in a chargetransfer interaction with the FAD prosthetic group [4,5]. Complexes with long-wavelength absorption are also formed between the enzyme and various acyl-CoA compounds, including acetoacetyl-CoA, which gives a grey-green complex with an absorbance maximum at 580 nm [6]. Butyryl-CoA dehydrogenase was purified from Megasphaera elsdenii as in [ 121. Coenzyme A was purchased from Sigma. Other reagents were from BDH.
収録刊行物
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- FEBS Letters
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FEBS Letters 138 29-32, 1982-02-08
Wiley