Literature DB >> 6292016

Characterisation of the electron transport chain of an obligate methylotroph, strain 4025.

M Vrdoljak, S Froud.   

Abstract

1. The obligate methanol-utilising bacterium strain 4025 contains cytochromes b and c. Cytochrome a is never present. 2. The soluble cytochrome c is similar to that from other methylotrophs in reacting (slowly) with carbon monoxide and it can be separated into two types, differing markedly in their isoelectric points. 3. Some of the cytochrome b reacts rapidly with carbon monoxide and is thus the likely cytochrome oxidase (cytochrome o). 4. The partially purified, NAD+-independent methanol dehydrogenase is similar to such enzymes from the other methanol-utilising bacteria in respect of its prosthetic group, dependence on ammonia or methylamine for activity and its wide substrate specificity. 5. The fluorescence seen in colonies of this organism is probably due to a flavin derivative. 6. This study of electron transport components does not shed any light on the unusually high copper requirement shown by this methylotroph.

Entities:  

Mesh:

Substances:

Year:  1982        PMID: 6292016     DOI: 10.1016/0020-711x(82)90063-5

Source DB:  PubMed          Journal:  Int J Biochem        ISSN: 0020-711X


  1 in total

1.  The 'methylamine oxidase' system of an obligate methylotroph.

Authors:  K A Auton; C Anthony
Journal:  Biochem J       Date:  1989-05-15       Impact factor: 3.857

  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.