Purification and characterization of the oxygenase component of biphenyl 2,3-dioxygenase from Pseudomonas sp. strain LB400.
The iron-sulfur protein of biphenyl 2,3-dioxygenase (ISPBPH) was purified from Pseudomonas sp. strain LB400. The protein is composed of a 1:1 ratio of a large (alpha) subunit with an estimated molecular weight of 53,300 and a small (beta) subunit with an estimated molecular weight of 27,300. The nat...
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| Published in: | J Bacteriol |
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| Main Authors: | , |
| Format: | Artigo |
| Language: | Inglês |
| Published: |
American Society for Microbiology (ASM)
1995
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| Subjects: | |
| Online Access: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC177406/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/7592331/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.177.20.5834-5839.1995 |
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