T7 RNA Polymerase Does Not Interact with the 5'-Phosphate of the Initiating Nucleotide
Craig T. Martin and Joseph E. Coleman, Biochemistry 28, 2760-2762, 1989 The study of transcription kinetics by T7 RNA polymerase is facilitated by the small size of its promoter, allowing the use of synthetic oligonucleotide templates with carefully defined sequences. We …
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T7 RNA Polymerase Interacts with Its Promoter from One Side of the DNA Helix
Daniel K. Muller, Craig T. Martin, and Joseph E. Coleman, Biochemistry 28, 3306-3313, 1989 The interactions of T7 RNA polymerase with its promoter DNA have been previously probed in footprinting experiments with either DNase I or (methidiumpropyl-EDTA)-Fe(II) to cleave unprotected DNA …
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On the nature of cysteine coordination to CuA in cytochrome c oxidase
C T Martin, C P Scholes, and S I Chan, Journal of Biological Chemistry 263, 8420-8429, 1988 The resolution of new features in the 1H electron nuclear double resonance (ENDOR) spectrum of the oxidized CuA site in beef heart cytochrome …
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Processivity in Early Stages of Transcription by T7 RNA Polymerase
Craig T. Martin, Daniel K. Muller, and Joseph E. Coleman, Biochemistry 27, 3966-3974, 1988 Immediately following initiation of transcription, T7 RNA polymerase enters a phase in which dissociation of the enzyme-DNA-RNA ternary complex significantly competes with elongation, a process referred to …
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Processivity of Proteolytically Modified Forms of T7 RNA Polymerase
Daniel K. Muller, Craig T. Martin, and Joseph E. Coleman, Biochemistry 27, 5763-5771, 1988 Two proteolytically modified forms of T7 RNA polymerase have been characterized with respect to transcription initiation and processivity. One species, denoted 80K-20K, is singly cleaved within the …
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Kinetic Analysis of T7 RNA Polymerase-Promoter Interactions with Small Synthetic Promoters
Craig T. Martin and Joseph E. Coleman, Biochemistry 26, 2690-2696, 1987 Specific interactions between T7 RNA polymerase and its promoter have been studied by asimple steady-state kinetic assay using synthetic oligonucleotide promoters that produce a short five-basemessage. A series of …
The identification of histidine ligands to cytochrome a in cytochrome c oxidase
Craig T. Martin, Charles P. Scholes, Sunney I. Chan, Journal of Biological Chemistry 260, 2857-2861, 1985 A histidine auxotroph of Saccharomyces cerevisiae has been used to metabolically incorporate [1,3-15N2] histidine into yeast cytochrome c oxidase. Electron nuclear double resonance (ENDOR) …
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The Energetics and Molecular Dynamics of the Proton Pumping Photocycle in Bacteriorhodopsin
Robert R. Birge, Albert F. Lawrence, Thomas M. Cooper, Craig T. Martin, David F. Blair, Sunney I. Chan, Nonlinear Electrodynamics in Biological Systems, 107-120, 1984 The energy stored in the primary photochemical event of light adapted bacteriorhodopsin (~16 kcal mol-1) …
The metal centers of cytochrome c oxidase: Structure and function
Sunney I. Chan, David F. Blair, Craig T. Martin, Hsin Wang, Jeff Gelles, JE Morgan, Steve Witt, RR Birge, Tom H. Stevens, Gary W. Brudvig, Inorganica Chimica Acta 79 72-73 1983 Considerable progress has been made in recent years on …
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A resonance Raman investigation of perturbed states of tree and fungal laccase
DF Blair, GW Campbell, V Lum, CT Martin, HB Gray, BG Malmström, Sunney I. Chan, Journal of Inorganic Biochemistry 19, 65-73 Resonance Raman (RR) spectra of Rhus vernicifera laccase and Polyporus versicolor laccase in several perturbed states are reported. Coordination of fluoride to the …
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The structure of the metal centers in cytochrome c oxidase
Sunney I. Chan, Craig T. Martin, Hsin Wang, Gary W. Brudvig, Tom H. Stevens, The Coordination Chemistry of Metalloenzymes, 313-328, 1983 Progress toward elucidation of the structure of the metal centers in cytochrome c oxidase will be reviewed. Our studies are based …
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The nature of CuA in cytochrome c oxidase
Tom H. Stevens, Craig T. Martin, Hsin Wang, Gary W. Brudvig, Charles P. Scholes, Sunney I. Chan, Journal of Biological Chemistry 257, 12106-12113, 1982 The isolation and purification of yeast cytochrome c oxidase is described. Characterization of the purified protein …
The nature and the distribution of the metal centers in cytochrome c oxidase
Chan, Sunney I; Brudvig, Gary W; Martin, Craig T; Stevens, Tom H; in: "Electron Transport and Oxygen Utilization" (C. Ho, ed.) Elsevier Publishing Co., Amsterdam Electron Transport and Oxygen Utilization 171-177 1982
METAL CENTERS OF CYTOCHROME c OXIDASE: STRUCTURES AND INTERACTIONS
David F. Blair, Craig T. Martin, Jeff Gelles, Hsin Wang, Gary W. Brudvig, Tom H. Stevens, Sunney I. Chan, Chemica Scripta 21, 43-53, 1981 Studies directed toward the elucidation of the structures of the metal centers in cytochrome c oxidase …
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Reactions of nitric oxide with tree and fungal laccase
Craig T. Martin, Randall H. Morse, Robert M. Kanne, Harry B. Gray, Bo G. Malmström, Sunney I. Chan, Biochemistry 20, 5147-5155, 1981 The reactions of nitric oxide (NO) with the oxi- dized and reduced forms of fungal and tree laccase, as well as with tree laccase depleted in type 2 copper, are reported. The products of the reactions were determined by NMR and mass spectroscopy, whereas the oxidation states of the enzymes were monitored by EPR and optical spectroscopy. All three copper sites in fungal lacease are reduced by NO. In addition,NO forms a specific complex with the reduced type 2 copper. NO similarly reduces all of the copper sites in tree lacease, but it also oxidizes the reduced sites produced by ascorbate or NO reduction. A catalytic cycle is set up in which N20, …
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