ATP synthases. Structure, reaction center, mechanism, and regulation of one of nature's most unique machines.
Pedersen
P L
PL
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
Amzel
L M
LM
D000595:Amino Acid Sequence; D000818:Animals; D002736:Chloroplasts / Q000201:enzymology; D004734:Energy Metabolism; D004926:Escherichia coli / Q000201:enzymology; D005658:Fungi / Q000201:enzymology; D046911:Macromolecular Substances; D008928:Mitochondria / Q000201:enzymology; D008954:Models, Biological; D008961:Models, Structural; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism*
D046911:Macromolecular Substances; D006180:Proton-Translocating ATPases