Cytochrome cM Is Probably a Membrane Protein Similar to the C Subunit of the Bacterial Nitric Oxide Reductase

• Published in: Applied sciences Vol. 11; no. 20; p. 9396
• Main Authors: Rodríguez-Gil, Tomás, Torrado, Alejandro, Iniesta-Pallarés, Macarena, Álvarez, Consolación, Mariscal, Vicente, Molina-Heredia, Fernando P.
• Format: Journal Article
• Language: English
• Published: Basel MDPI AG 01.10.2021
• Subjects: Binding sites; Cyanobacteria; Cytochrome; cytochrome cM; E coli; Genes; Genomes; Hypotheses; Membrane proteins; Membranes; Nitric oxide; Nitric-oxide reductase; NorC; Nucleotide sequence; Peptides; Photosynthesis; Physiology; Proteins; Reductases; Respiration
• DOI: 10.3390/app11209396
• ISSN: 2076-3417

Cytochrome cM was first described in 1994 and its sequence has been found in the genome of manifold cyanobacterial species ever since. Numerous studies have been carried out with the purpose of determining its function, but none of them has given place to conclusive results so far. Many of these studies are based on the assumption that cytochrome cM is a soluble protein located in the thylakoid lumen of cyanobacteria. In this work, we have reevaluated the sequence of cytochrome cM, with our results showing that its most probable 3D structure is strongly similar to that of the C subunit of the bacterial nitric oxide reductase. The potential presence of an α-helix tail, which could locate this protein in the thylakoid membrane, further supports this hypothesis, thus providing a new, unexpected role for this redox protein.