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A resonance Raman study on the nature of charge‐transfer interactions in butyryl CoA dehydrogenase
Author(s) -
Williamson Gary,
Engel Paul C.,
Nishina Yasuzo,
Shiga Kiyoshi
Publication year - 1982
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(82)80387-6
Subject(s) - okazaki fragments , chemistry , library science , computer science , biochemistry , eukaryotic dna replication , dna repair , gene
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.