cytochrome-c-t and heme-d1

cytochrome-c-t has been researched along with heme-d1* in 1 studies

Other Studies

1 other study(ies) available for cytochrome-c-t and heme-d1

ArticleYear
Crystal Structure of Dihydro-Heme d
    Journal of molecular biology, 2019, 08-09, Volume: 431, Issue:17

    Many bacteria can switch from oxygen to nitrogen oxides, such as nitrate or nitrite, as terminal electron acceptors in their respiratory chain. This process is called "denitrification" and enables biofilm formation of the opportunistic human pathogen Pseudomonas aeruginosa, making it more resilient to antibiotics and highly adaptable to different habitats. The reduction of nitrite to nitric oxide is a crucial step during denitrification. It is catalyzed by the homodimeric cytochrome cd

    Topics: Amino Acids; Bacterial Proteins; Binding Sites; Catalysis; Cytochromes c; Heme; Humans; Models, Molecular; Nitric Oxide; Nitrite Reductases; Nitrites; Oxidation-Reduction; Oxidoreductases; Protein Conformation; Protein Domains; Pseudomonas aeruginosa; Transition Temperature

2019