Search Results - "Sanders-Loehr"

The Catalytic Center in Nitrous Oxide Reductase, Cu Z , Is a Copper−Sulfide Cluster by Rasmussen, Tim, Berks, Ben C., Sanders-Loehr, Joann, Dooley, David M., Zumft, Walter G., Thomson, Andrew J.

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Characterization of the Copper−Sulfur Chromophores in Nitrous Oxide Reductase by Resonance Raman Spectroscopy:  Evidence for Sulfur Coordination in the Catalytic Cluster by Alvarez, Marcela L, Ai, Jingyuan, Zumft, Walter, Sanders-Loehr, Joann, Dooley, David M

“…Nitrous oxide reductase (N2OR) from Pseudomonas stutzeri, a dimeric enzyme with a canonical metal ion content of at least six Cu ions per subunit, contains two…”
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Glyoxal Oxidase from Phanerochaete chrysosporium Is a New Radical-Copper Oxidase (∗) by Whittaker, Mei M., Kersten, Philip J., Nakamura, Nobuhumi, Sanders-Loehr, Joann, Schweizer, Elizabeth S., Whittaker, James W.

“…A free radical-coupled copper complex has been identified as the catalytic structure in the active site of glyoxal oxidase from Phanerochaete chrysosporium…”
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Copper(2+) Binding to the Surface Residue Cysteine 111 of His46Arg Human Copper−Zinc Superoxide Dismutase, a Familial Amyotrophic Lateral Sclerosis Mutant by Liu, Hongbin, Zhu, Haining, Eggers, Daryl K, Nersissian, Aram M, Faull, Kym F, Goto, Joy J, Ai, Jingyuan, Sanders-Loehr, Joann, Gralla, Edith Butler, Valentine, Joan Selverstone

“…Mutations in copper−zinc superoxide dismutase (CuZnSOD) cause 25% of familial amyotrophic lateral sclerosis (FALS) cases. This paper examines one such mutant,…”
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Loop-Directed Mutagenesis of the Blue Copper Protein Amicyanin from Paracoccus versutus and Its Effect on the Structure and the Activity of the Type-1 Copper Site by Buning, Christian, Canters, Gerard W, Comba, Peter, Dennison, Christopher, Jeuken, Lars, Melter, Michael, Sanders-Loehr, Joann

“…Four loop-mutants of the blue copper protein amicyanin from Paracoccus versutus have been constructed and characterized. The mutations replaced the loop…”
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An Unexpected Role for the Active Site Base in Cofactor Orientation and Flexibility in the Copper Amine Oxidase from Hansenula polymorpha by Plastino, Julie, Green, Edward L, Sanders-Loehr, Joann, Klinman, Judith P

“…The role of the active site aspartate base in the aminotransferase mechanism of the copper amine oxidase from the yeast Hansenula polymorpha has been probed by…”
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Rack-Induced Metal Binding vs. Flexibility: Met121His Azurin Crystal Structures at Different pH by Messerschmidt, Albrecht, Prade, Lars, Kroes, Sandra J., Sanders-Loehr, Joann, Huber, Robert, Canters, Gerard W.

“…The rack-induced bonding mechanism of metals to proteins is a useful concept for explaining the generation of metal sites in electron transfer proteins, such…”
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N-Isotope effects on the Raman spectra of Fe2S2 ferredoxin and Rieske ferredoxin: evidence for structural rigidity of metal sites by Rotsaert, Frederik A., Pikus, Jeremie D., Fox, Brian G., Markley, John L., Sanders-Loehr, Joann

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Resonance Raman Evidence for an Fe-O-Fe Center in Stearoyl-ACP Desaturase. Primary Sequence Identity with Other Diiron-Oxo Proteins by Fox, Brian G, Shanklin, John, Ai, Jingyuan, Loehr, Thomas M, Sanders-Loehr, Joann

“…The stearoyl-ACP delta 9 desaturase from plants is a new example of a growing number of proteins that contain oxo- or hydroxo-bridged diiron clusters. On the…”
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A Hemerythrin-like Domain in a Bacterial Chemotaxis Protein by Xiong, Junjie, Kurtz, Donald M, Ai, Jingyuan, Sanders-Loehr, Joann

“…Hemerythrin (Hr) is an O2-carrying protein found in some marine invertebrates. A conserved sequence motif in all Hrs provides five histidine and two…”
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Dioxygen is the source of the mu-oxo bridge in iron ribonucleotide reductase by JINSHU LING, SAHLIN, M, SJÖBERG, B.-M, LOEHR, T. M, SANDERS-LOEHR, J

“…The formation of the iron-radical cofactor in the R2 subunit of ribonucleotide reductase has been monitored by resonance Raman spectroscopy. The differrous…”
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The environment of Fe4S4 clusters in ferredoxins and high-potential iron proteins. New information from x-ray crystallography and resonance Raman spectroscopy by Backes, Gabriele, Mino, Yoshiki, Loehr, Thomas M, Meyer, Terrence E, Cusanovich, Michael A, Sweeney, William V, Adman, Elinor T, Sanders-Loehr, Joann

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Characterization of the Native Lysine Tyrosylquinone Cofactor in Lysyl Oxidase by Raman Spectroscopy by Wang, Sophie X., Nakamura, Nobuhumi, Mure, Minae, Klinman, Judith P., Sanders-Loehr, Joann

“…Lysine tyrosylquinone (LTQ) recently has been identified as the active site cofactor in lysyl oxidase by isolation and characterization of a derivatized active…”
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The crystal structures of Phascolopsis gouldii wild type and L98Y methemerythrins: structural and functional alterations of the O2 binding pocket by Farmer, C S, Kurtz, Jr, D M, Liu, Z J, Wang, B C, Rose, J, Ai, J, Sanders-Loehr, J

“…Reported are the X-ray crystal structures of recombinant Phascolopsis gouldii methemerythrin (1.8-A resolution) and the structure of an O2-binding-pocket…”
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Relationship between Conserved Consensus Site Residues and the Productive Conformation for the TPQ Cofactor in a Copper-Containing Amine Oxidase from Yeast by Schwartz, Benjamin, Green, Edward L, Sanders-Loehr, Joann, Klinman, Judith P

“…A highly conserved asparagine residue is contained in the consensus site sequences of all known copper-containing amine oxidases (CAOs). On the basis of…”
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Common Oxygen Binding Site in Hemocyanins from Arthropods and Mollusks. Evidence from Raman Spectroscopy and Normal Coordinate Analysis by Ling, Jinshu, Nestor, Lisa P, Czernuszewicz, Roman S, Spiro, Thomas G, Fraczkiewicz, Robert, Sharma, Kamala D, Loehr, Thomas M, Sanders-Loehr, Joann

“…Resonance Raman (RR) spectra of oxyhemocyanins (oxyHcs) from an arthropod (Limulus polyphemus) and two mollusks (Busycon canaliculatum and Octopus dofleini)…”
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A new type 2 copper cysteinate azurin. Involvement of an engineered exposed cysteine in copper binding through internal rearrangement by van Amsterdam, Irene M C, Ubbink, Marcellus, van den Bosch, Marieke, Rotsaert, Frederik, Sanders-Loehr, Joann, Canters, Gerard W

“…The double mutant H117G/N42C azurin exhibits tetragonal type 2 copper site characteristics with Cys(42) as one of the copper ligands as concluded from…”
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A leucine residue "Gates" solvent but not O2 access to the binding pocket of phascolopsis gouldii hemerythrin by Farmer, C S, Kurtz, Jr, D M, Phillips, R S, Ai, J, Sanders-Loehr, J

“…A leucine residue, Leu-98, lines the O(2)-binding pocket in all known hemerythrins. Leu-98 in recombinant Phascolopsis gouldii hemerythrin, was mutated to…”
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Rates of Oxygen and Hydrogen Exchange as Indicators of TPQ Cofactor Orientation in Amine Oxidases by Green, Edward L, Nakamura, Nobuhumi, Dooley, David M, Klinman, Judith P, Sanders-Loehr, Joann

“…This study presents the first detailed examination by resonance Raman (RR) spectroscopy of the rates of solvent exchange for the C5 and C3 positions of the TPQ…”
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Electronic and Raman spectroscopic properties of oxo-bridged dinuclear iron centers in proteins and model compounds by Sanders-Loehr, Joann, Wheeler, William D, Shiemke, Andrew K, Averill, Bruce A, Loehr, Thomas M

“…Oxo-bridged dinuclear Fe(III) complexes generally exhibit a strongly enhanced Fe-O-Fe symmetric stretching vibration in their resonance Raman spectra upon…”
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