Mutational and biochemical analysis of cytochrome c', a nitric oxide-binding lipoprotein important for adaptation of Neisseria gonorrhoeae to oxygen-limited growth

• Published in: Biochemical journal Vol. 388; no. Pt 2; pp. 545 - 553
• Main Authors: Turner, Susan M, Moir, James W B, Griffiths, Lesley, Overton, Timothy W, Smith, Harry, Cole, Jeff A
• Format: Journal Article
• Language: English
• Published: England Portland Press Ltd 01.06.2005
• Subjects: Adaptation, Physiological; Cytochromes c' - chemistry; Cytochromes c' - metabolism; Escherichia coli; Escherichia coli - genetics; Gene Expression Regulation, Bacterial; Gene Expression Regulation, Enzymologic; Lipoproteins - chemistry; Mutagenesis, Site-Directed; Neisseria gonorrhoeae; Neisseria gonorrhoeae - enzymology; Neisseria gonorrhoeae - genetics; Neisseria gonorrhoeae - growth & development; Nitric Oxide - metabolism; Nitrites - metabolism; Oxygen - physiology; Phenotype; Protein Binding; Protein Processing, Post-Translational

Neisseria gonorrhoeae is a prolific source of c-type cytochromes. Five of the constitutively expressed cytochromes are predicted, based on in silico analysis of the N. gonorrhoeae genome, to be components of the cytochrome bc1 complex, cytochrome c oxidase cbb3 or periplasmic cytochromes involved in...