Grubmeyer C - Search Results

1

The stereochemical course of phosphoric residue transfer catalyzed by beef heart mitochondrial ATPase.

Webb MR, Grubmeyer C, Penefsky HS, Trentham DR. Webb MR, et al. Among authors: grubmeyer c. J Biol Chem. 1980 Dec 25;255(24):11637-9. J Biol Chem. 1980. PMID: 6449510 Free article.

2

Mechanism of ATP hydrolysis by beef heart mitochondrial ATPase. Rate constants for elementary steps in catalysis at a single site.

Grubmeyer C, Cross RL, Penefsky HS. Grubmeyer C, et al. J Biol Chem. 1982 Oct 25;257(20):12092-100. J Biol Chem. 1982. PMID: 6214557 Free article. No abstract available.

3

Mechanism of ATP hydrolysis by beef heart mitochondrial ATPase. Rate enhancements resulting from cooperative interactions between multiple catalytic sites.

Cross RL, Grubmeyer C, Penefsky HS. Cross RL, et al. Among authors: grubmeyer c. J Biol Chem. 1982 Oct 25;257(20):12101-5. J Biol Chem. 1982. PMID: 6214558 Free article. No abstract available.

4

The presence of two hydrolytic sites on beef heart mitochondrial adenosine triphosphatase.

Grubmeyer C, Penefsky HS. Grubmeyer C, et al. J Biol Chem. 1981 Apr 25;256(8):3718-27. J Biol Chem. 1981. PMID: 6452454 Free article.

5

Cooperatively between catalytic sites in the mechanism of action of beef heart mitochondrial adenosine triphosphatase.

Grubmeyer C, Penefsky HS. Grubmeyer C, et al. J Biol Chem. 1981 Apr 25;256(8):3728-34. J Biol Chem. 1981. PMID: 6452455 Free article.

Addition of excess nonradioactive TNP-ATP, in concentrations sufficient to fill catalytic Site 2 on the enzyme (Grubmeyer, C., and Penefsky, H. S. (1981) J. Biol. Chem. 256, 3718-3727), accelerates the rate of hydrolysis of the radioactive substrate 15- to 20-fold. …

Addition of excess nonradioactive TNP-ATP, in concentrations sufficient to fill catalytic Site 2 on the enzyme (Grubmeyer, C., …

6

Evidence for catalytic cooperativity during ATP hydrolysis by beef heart F1-ATPase. Kinetics and binding studies with the photoaffinity label BzATP.

Ackerman SH, Grubmeyer C, Coleman PS. Ackerman SH, et al. Among authors: grubmeyer c. J Biol Chem. 1987 Oct 5;262(28):13765-72. J Biol Chem. 1987. PMID: 2888764 Free article.

7

A new paradigm for biochemical energy coupling. Salmonella typhimurium nicotinate phosphoribosyltransferase.

Vinitsky A, Grubmeyer C. Vinitsky A, et al. Among authors: grubmeyer c. J Biol Chem. 1993 Dec 5;268(34):26004-10. J Biol Chem. 1993. PMID: 7503993 Free article.

8

L-histidinol dehydrogenase, a Zn2+-metalloenzyme.

Grubmeyer C, Skiadopoulos M, Senior AE. Grubmeyer C, et al. Arch Biochem Biophys. 1989 Aug 1;272(2):311-7. doi: 10.1016/0003-9861(89)90224-5. Arch Biochem Biophys. 1989. PMID: 2665648

9

Kinetic mechanism of orotate phosphoribosyltransferase from Salmonella typhimurium.

Bhatia MB, Vinitsky A, Grubmeyer C. Bhatia MB, et al. Among authors: grubmeyer c. Biochemistry. 1990 Nov 20;29(46):10480-7. doi: 10.1021/bi00498a009. Biochemistry. 1990. PMID: 2271660

10

Cloning and nucleic acid sequence of the Salmonella typhimurium pncB gene and structure of nicotinate phosphoribosyltransferase.

Vinitsky A, Teng H, Grubmeyer CT. Vinitsky A, et al. Among authors: grubmeyer ct. J Bacteriol. 1991 Jan;173(2):536-40. doi: 10.1128/jb.173.2.536-540.1991. J Bacteriol. 1991. PMID: 1987148 Free PMC article.

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