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

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 stu...

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Bibliographic Details
Published inApplied 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
LanguageEnglish
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
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Summary: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.
ISSN:2076-3417
2076-3417
DOI:10.3390/app11209396