Literature summary for 7.1.2.2 extracted from

Chen, W.; Hu, C.Y.; Crampton, D.J.; Frasch, W.D.
Characterization of the metal binding environment of catalytic site 1 of chloroplast F1-ATPase from Chlamydomonas (2000), Biochemistry, 39, 9393-9400.

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Protein Variants

Protein Variants	Comment	Organism
D262C	modification of beta-subunit, mutation causes large changes in the 51V hyperfine tensor of VO2+-nucleotide bound to site 1	Chlamydomonas reinhardtii
D262H	modification of beta-subunit, mutation causes large changes in the 51V hyperfine tensor of VO2+-nucleotide bound to site 1	Chlamydomonas reinhardtii
D262T	modification of beta-subunit, mutation causes large changes in the 51V hyperfine tensor of VO2+-nucleotide bound to site 1	Chlamydomonas reinhardtii
E197C	modification of beta-subunit, mutation impairs ATP synthase and ATPase activity catalyzed by CF1F0 and soluble CF1 respectively. Mutation causes large changes in the 51V hyperfine tensor of VO2+-nucleotide bound to site 1 but not to site 3	Chlamydomonas reinhardtii
E197D	modification of beta-subunit, mutation impairs ATP synthase and ATPase activity catalyzed by CF1F0 and soluble CF1 respectively. Mutation causes large changes in the 51V hyperfine tensor of VO2+-nucleotide bound to site 1 but not to site 3	Chlamydomonas reinhardtii
E197S	modification of beta-subunit, mutation impairs ATP synthase and ATPase activity catalyzed by CF1F0 and soluble CF1 respectively. Mutation causes large changes in the 51V hyperfine tensor of VO2+-nucleotide bound to site 1 but not to site 3	Chlamydomonas reinhardtii

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

Organism	UniProt	Comment	Textmining
Chlamydomonas reinhardtii	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O + H+/in	-	Chlamydomonas reinhardtii	ADP + phosphate + H+/out	-	?

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Release 2023.1 (January 2023)