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Mutagenesis of the gene encoding amicyanin of Paracoccus denitrificans and the resultant effect on methylamine oxidation.
Department of Microbiology, Vrije Universiteit, Amsterdam, The Netherlands.
The gene encoding the blue-copper protein amicyanin was isolated from a genomic bank of Paracoccus denitrificans by using a synthetic oligonucleotide. It is located directly downstream of the gene encoding the small subunit of methylamine dehydrogenase. Amicyanin is transcribed as a precursor protein with a signal sequence, typical for periplasmic proteins. Specific inactivation of amicyanin by means of gene replacement techniques resulted in the complete loss of the ability to grow on methylamine.
PMID: 2261991 [PubMed - indexed for MEDLINE]
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Cited by 18 PubMed Central articles
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The axial ligand and extent of protein folding determine whether Zn or Cu binds to amicyanin.
Ma JK, Lee S, Choi M, Bishop GR, Hosler JP, Davidson VL.
J Inorg Biochem. 2008 Feb; 102(2):342-6. Epub 2007 Oct 1.
[J Inorg Biochem. 2008]
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Cytochromes c(550), c(552), and c(1) in the electron transport network of Paracoccus denitrificans: redundant or subtly different in function?
Otten MF, van der Oost J, Reijnders WN, Westerhoff HV, Ludwig B, Van Spanning RJ.
J Bacteriol. 2001 Dec; 183(24):7017-26.
[J Bacteriol. 2001]
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Heterologous expression of correctly assembled methylamine dehydrogenase in Rhodobacter sphaeroides.
Graichen ME, Jones LH, Sharma BV, van Spanning RJ, Hosler JP, Davidson VL.
J Bacteriol. 1999 Jul; 181(14):4216-22.
[J Bacteriol. 1999]
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