Search Results - "Goodin, D B"

Multifrequency High-Field EPR Study of the Tryptophanyl and Tyrosyl Radical Intermediates in Wild-Type and the W191G Mutant of Cytochrome c Peroxidase by Ivancich, Anabella, Dorlet, Pierre, Goodin, David B, Un, Sun

“…Multifrequency (95, 190, and 285 GHz) high-field electron paramagnetic resonance (EPR) spectroscopy has been used to characterize radical intermediates in…”
Get full text

Identification by ENDOR of Trp191 as the free-radical site in cytochrome c peroxidase compound ES by MOHANRAM SIVARAJA, GOODIN, D. B, SMITH, M, HOFFMAN, B. M

“…The chemical identity of the amino acid free-radical site that represents one of the two oxidizing equivalents stored in the H2O2-oxidized intermediate…”
Get full text

Replacement of the Axial Histidine Ligand with Imidazole in Cytochrome c Peroxidase. 2. Effects on Heme Coordination and Function by Hirst, Judy, Wilcox, Sheri K, Ai, Jingyuan, Moënne-Loccoz, Pierre, Loehr, Thomas M, Goodin, David B

“…The inability of imidazole to complement function in the axial histidine deletion mutant, H175G, of yeast cytochrome c peroxidase has been an intriguing but…”
Get full text

Construction of a bisaquo heme enzyme and binding by exogenous ligands by McRee, D E, Jensen, G M, Fitzgerald, M M, Siegel, H A, Goodin, D B

“…The crystal structure of the His-175-->Gly (H175G) mutant of cytochrome-c peroxidase (EC 1.11.1.5), missing its only heme ligand, reveals that the histidine is…”
Get full text

Energetics of Cation Radical Formation at the Proximal Active Site Tryptophan of Cytochrome c Peroxidase and Ascorbate Peroxidase by Jensen, G. M, Bunte, S. W, Warshel, A, Goodin, D. B

“…Despite very similar protein structures, ascorbate peroxidase (APX) and yeast cytochrome c peroxidase (CCP) stabilize different radical species during enzyme…”
Get full text

Impact of proximal and distal pocket site-directed mutations on the ferric/ferrous heme redox potential of yeast cytochrome c peroxidase by Jensen, G. M., Goodin, D. B.

“…Cytochrome c peroxidase (CCP) contains a five-coordinate heme active site. The reduction potential for the ferric to ferrous couple in CCP is anomalously low…”
Get full text

Small Molecule Binding to an Artificially Created Cavity at the Active Site of Cytochrome c Peroxidase by Fitzgerald, Melissa M, Churchill, Michael J, McRee, Duncan E, Goodin, David B

“…In the oxidized "ES" state of cytochrome c peroxidase, Trp-191 is reversibly oxidized to a stable cation free radical by the hypervalent heme. To explore the…”
Get full text

Comprehensive explanation of the anomalous EPR spectra of wild-type and mutant cytochrome c peroxidase compound ES by Houseman, Andrew L. P, Doan, Peter E, Goodwin, David B, Hoffman, Brian M

“…Although the cytochrome c peroxidase/H2O2 reaction product, compound ES, has been a long-standing subject of research, only recently has its broad EPR signal…”
Get full text

Copper Binding to the Prion Protein: Structural Implications of Four Identical Cooperative Binding Sites by Viles, John H., Cohen, Fred E., Prusiner, Stanely B., Goodin, David B., Wright, Peter E., Dyson, H. Jane

“…Evidence is growing to support a functional role for the prion protein (PrP) in copper metabolism. Copper ions appear to bind to the protein in a highly…”
Get full text

Oxidized and Reduced Azotobacter vinelandii Ferredoxin I at 1.4 Å Resolution:  Conformational Change of Surface Residues without Significant Change in the [3Fe-4S]+/0 Cluster by Schipke, C. G, Goodin, D. B, McRee, D. E, Stout, C. D

“…The refined structure of reduced Azotobacter vinelandii 7Fe ferredoxin FdI at 100 K and 1.4 Å resolution is reported, permitting comparison of [3Fe-4S]+ and…”
Get full text

The peroxide complex of yeast cytochrome c peroxidase contains two distinct radical species, neither of which resides at methionine 172 or tryptophan 51 by Goodin, D B, Mauk, A G, Smith, M

“…The nature of the free radical species observed in the peroxide complex of yeast cytochrome c peroxidase is described for protein variants containing amino…”
Get full text

Protein conformer selection by ligand binding observed with crystallography by Cao, Yi, Musah, Rabi A., Wilcox, Sheri K., Goodin, David B., McRee, Duncan E.

“…A large‐scale movement between “closed” and “open” conformations of a protein loop was observed directly with protein crystallography by trapping individual…”
Get full text

Density Functional and MP2 Calculations of Spin Densities of Oxidized 3-Methylindole:  Models for Tryptophan Radicals by Jensen, G. M, Goodin, D. B, Bunte, S. W

“…Ab initio calculations have been carried out on 3-methylindole, and the cation and neutral radicals of 3-methylindole, using density functional theory (DFT),…”
Get full text

Amino acid substitutions at tryptophan-51 of cytochrome c peroxidase: effects on coordination, species preference for cytochrome c, and electron transfer by Goodin, David B, Davidson, Marilyn G, Roe, James A, Mauk, A. Grant, Smith, Michael

“…Amino acid replacements of an aromatic residue, Trp-51, which is in contact with the heme of yeast cytochrome c peroxidase have a number of significant effects…”
Get full text

The Asp-His-Fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free radical to the heme by Goodin, D B, McRee, D E

“…The buried charge of Asp-235 in cytochrome c peroxidase (CCP) forms an important hydrogen bond to the histidine ligand of the heme iron. The Asp-His-metal…”
Get full text

The role of aspartate‐235 in the binding of cations to an artificial cavity at the radical site of cytochrome c peroxidase by Fitzgerald, Melissa M., Trester, Michelle L., Jensen, Gerard M., Mcree, Duncan E., Goodin, David B.

“…The activated state of cytochrome c peroxidase, compound ES, contains a cation radical on the Trp‐191 side chain. We recently reported that replacing this…”
Get full text

Studies of the Radical Species in Compound ES of Cytochrome c Peroxidase Altered by Site-Directed Mutagenesis by Goodin, David B., Mauk, A. Grant, Smith, Michael

“…Yeast cytochrome c peroxidase reacts with hydrogen peroxide to form an intermediate, compound ES, in which the heme iron atom is converted to a ferryl function…”
Get full text

Conformational States of Cytochrome P450cam Revealed by Trapping of Synthetic Molecular Wires by Hays, Anna-Maria A., Dunn, Alexander R., Chiu, Richard, Gray, Harry B., Stout, C. David, Goodin, David B.

“…Members of the ubiquitous cytochrome P450 family catalyze a vast range of biologically significant reactions in mammals, plants, fungi, and bacteria. Some…”
Get full text

Enhanced oxidation of aniline derivatives by two mutants of cytochrome c peroxidase at tryptophan 51 by ROE, J. A, GOODIN, D. B

“…Two hyperactive mutants of cytochrome c peroxidase (CCP), W51F and W51A, catalyze the enhanced oxidation of a number of substituted anilines. The reaction of…”
Get full text

Identification of a Porphyrin .pi. Cation Radical in Ascorbate Peroxidase Compound I by Patterson, William R, Poulos, Thomas L, Goodin, David B

“…Electron paramagnetic resonance (EPR) spectroscopy has been used to analyze the ascorbate peroxidase Fe3+ resting state and to compare the reaction product…”
Get full text