The use of 8-azido-ATP and 8-azido-ADP as photoaffinity labels of the ATP synthase in submitochondrial particles: evidence for a mechanism of ATP hydrolysis involving two independent catalytic sites?

scientific article published on August 1985

The use of 8-azido-ATP and 8-azido-ADP as photoaffinity labels of the ATP synthase in submitochondrial particles: evidence for a mechanism of ATP hydrolysis involving two independent catalytic sites? is …

instance of (P31):

scholarly article

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P356	DOI	10.1016/0005-2728(85)90163-X
P698	PubMed publication ID	2862913

P2093	author name string	J A Berden
		A Kemp
		M A Herweijer
		J B Sloothaak
P433	issue	1
P407	language of work or name	English	Q1860
P304	page(s)	27-38
P577	publication date	1985-08-01
P1433	published in	Biochimica et Biophysica Acta	Q864239
P1476	title	The use of 8-azido-ATP and 8-azido-ADP as photoaffinity labels of the ATP synthase in submitochondrial particles: evidence for a mechanism of ATP hydrolysis involving two independent catalytic sites?
P478	volume	809

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cites work (P2860)

Q42202677	1H-NMR studies on nucleotide binding to the catalytic sites of bovine mitochondrial F1-ATPase.
Q36995302	ATP synthase and the actions of inhibitors utilized to study its roles in human health, disease, and other scientific areas
Q59195068	Characterization of the respiratory chain from cultured Crithidia fasciculata
Q48371000	Cloning and characterization of the subunits comprising the catalytic core of the Trypanosoma brucei mitochondrial ATP synthase
Q42861906	Interaction of Mg2+ with F0.F1 mitochondrial ATPase as related to its slow active/inactive transition
Q95304591	One of the non-exchangeable nucleotides of the mitochondrial F1-ATPase is bound at a beta-subunit: evidence for a non-rotatory two-site catalytic mechanism
Q69871434	Steady-state kinetics of F1-ATPase. Mechanism of anion activation

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