Open AccessRegulation of nitrite resistance of the cytochrome cbb 3 oxidase by cytochrome c ScyA in Shewanella oneidensis
Author(s) -
Yin Jianhua,
Jin Miao,
Zhang Haiyan,
Ju Lili,
Zhang Lili,
Gao Haichun
Publication year - 2015
Publication title -
microbiologyopen
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.881
H-Index - 36
ISSN - 2045-8827
DOI - 10.1002/mbo3.224
Subject(s) - shewanella oneidensis , electron transport chain , cytochrome c oxidase , nitrite reductase , cytochrome , oxidase test , shewanella , electron transport complex iv , biochemistry , nitrite , cytochrome c , chemistry , heme , cytochrome b , respiratory chain , biology , enzyme , gene , bacteria , mitochondrion , genetics , mitochondrial dna , nitrate reductase , organic chemistry , nitrate
Cytochrome c proteins, as enzymes to exchange electrons with substrates or as pure electron carriers to shuttle electrons, play vital roles in bacterial respiration and photosynthesis. In Shewanella oneidensis , a research model for the respiratory diversity, at least 42 c ‐type cytochromes are predicted to be encoded in the genome and are regarded to be the foundation of its highly branched electron transport pathways. However, only a small number of c ‐type cytochromes have been extensively studied. In this study, we identify soluble cytochrome c ScyA as an important factor influencing the nitrite resistance of a strain devoid of the bd oxidase by utilizing a newly developed transposon mutagenesis vector, which enables overexpression of the gene(s) downstream of the insertion site. We show that when in overabundance ScyA facilitates growth against nitrite inhibition by enhancing nitrite resistance of the cbb 3 oxidase. Based on the data presented in this study, we suggest two possible mechanisms underlying the observed effect of ScyA: (1) ScyA increases electron flow to the cbb 3 oxidase; (2) ScyA promotes nitrite resistance of the cbb 3 oxidase, possibly by direct interaction.