Two distinct azurins function in the electron-transport chain of the obligate methylotroph Methylomonas J
- 15 July 1989
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 261 (2) , 495-499
- https://doi.org/10.1042/bj2610495
Abstract
Methylomonas J is an obligate methylotroph although it is unable to grow on methane. Like Pseudomonas AM1, it produces two blue copper proteins when growing on methylamine, one of which is the recipient of electrons from the methylamine dehydrogenase. When grown on methanol, only the other blue copper protein is produced. We have determined the amino acid sequences of these blue copper proteins, and show that they are both true azurins. The sequences are clearly homologous to those of the proteins characterized from fluorescent pseudomonads and various species of Alcaligenes, and can be aligned with them and with each other without the need to postulate any internal insertions or deletions in the sequences. The iso-1 azurin, the one produced during both methanol and methylamine growth, shows 59-65% identity with these other azurins, whereas the iso-2 protein shows only 47-53% identity. The proteins show 52% identitiy with each other. The two functionally equivalent blue copper proteins from Pseudomonas AM1 belong to two sequence classes that are quite distinct from the true azurins. Detailed evidence for the amino acid sequences of the proteins has been deposited as Supplementary Publication SUP 50151 (23 pages) at the British Library Document Supply Centre, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1989) 257, 5.This publication has 21 references indexed in Scilit:
- The crystal structure of pseudoazurin from Alcaligenes faecalis S‐6 determined at 2.9 Å resolutionFEBS Letters, 1987
- The amino acid sequence of the blue copper protein of Alcaligenes faecalisFEBS Letters, 1986
- The phylogeny of purple bacteria: The alpha subdivisionSystematic and Applied Microbiology, 1984
- Structure of azurin from Alcaligenes denitrificans at 2·5 Å resolutionJournal of Molecular Biology, 1983
- Amicyanin: An electron acceptor of methylamine dehydrogenaseBiochemical and Biophysical Research Communications, 1981
- Purification and properties of Paracoccus denitrificans azurinArchives of Biochemistry and Biophysics, 1980
- A crystallographic model for azurin at 3 Å resolutionJournal of Molecular Biology, 1978
- Methylamine dehydrogenase of Pseudomonas sp. J. Isolation and properties of the subunitsBiochimica et Biophysica Acta (BBA) - Enzymology, 1978
- Methylamine dehydrogenase of Pseudomonas sp. J. Purification and propertiesBiochimica et Biophysica Acta (BBA) - Enzymology, 1978
- Azurin: A Copper Protein Found in BordetellaJournal of General Microbiology, 1963