Výsledky vyhledávání - "Melanie M. Werst"

Detection of two histidyl ligands to CuA of cytochrome oxidase by 35-GHz ENDOR. 14,15N and 63,65Cu ENDOR studies of the CuA site in bovine heart cytochrome aa3 and cytochromes caa3 and ba3 from Thermus thermophilus

Autor: Melanie M. Werst, Ryszard J. Gurbiel, Yang C. Fann, Sunney I. Chan, Kristene K. Surerus, Siegfried M. Musser, James A. Fee, Brian M. Hoffman, Peter E. Doan

Publikováno v: Journal of the American Chemical Society. 115:10888-10894

To study the ligation of the Cu[sub A] site of heme-copper terminal oxidases, we have performed ENDOR measurements at X-band (9-GHz) and 35-GHz microwave frequencies on the three titled enzymes. The 35-GHz measurements provide complete spectral separ

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::810e36f405cfb8ea606c118e71823465
https://doi.org/10.1021/ja00076a053

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Nitrogen-14,15, carbon-13, iron-57, and proton-deuterium Q-band ENDOR study of iron-sulfur proteins with clusters that have endogenous sulfur ligands

Autor: John L. Markley, Chaoliang Fan, Melanie M. Werst, Mary Claire Kennedy, Byung-Ha Oh, Andrew L. P. Houseman, Helmut Beinert, Brian M. Hoffman

Publikováno v: Biochemistry. 31:2073-2080

The benefits of performing ENDOR experiments at higher microwave frequency are demonstrated in a Q-band (35 GHz) ENDOR investigation of a number of proteins with [nFe-mS] clusters, n = 2, 3, 4. Each protein displays several resonances in the frequenc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::71b16554d5376d2f1f26b974572c1123
https://doi.org/10.1021/bi00122a026

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Oxygen-17, proton, and deuterium electron nuclear double resonance characterization of solvent, substrate, and inhibitor binding to the iron-sulfur [4Fe-4S]+ cluster of aconitase

Autor: Brian M. Hoffman, Melanie M. Werst, Mary Claire Kennedy, Helmut Beinert

Publikováno v: Biochemistry. 29:10526-10532

{sup 17}O electron nuclear double resonance (ENDOR) studies at X-band (9-GHz) and Q-band (35-GHz) microwave frequencies reveal that the (4Fe-4S){sup {plus}} cluster of substrate-free aconitase (citrate (isocitrate) hydro-lyase, EC 4.2.1.3) binds solv

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c04b11005e05f510445939231342b26b
https://doi.org/10.1021/bi00498a015

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Characterization of the iron-sulfur [4Fe-4S]+ cluster at the active site of aconitase by iron-57, sulfur-33, and nitrogen-14 electron nuclear double resonance spectroscopy

Autor: Helmut Beinert, Melanie M. Werst, Mary Claire Kennedy, Andrew L. P. Houseman, Brian M. Hoffman

Publikováno v: Biochemistry. 29:10533-10540

57Fe, 33S, and 14N electron nuclear double resonance (ENDOR) studies have been performed to characterize the [4Fe-4S]+ cluster at the active site of aconitase. Q-band 57Fe ENDOLR of isotopically enriched enzyme, both substrate free and in the enzyme-

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::5ca95c56da4d3864d3e310c99a1397f3
https://doi.org/10.1021/bi00498a016

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Cytochrome c Oxidase: A Brief Introduction and Some New Results from High Field Endor Studies of The CuA and CuB Sites

Autor: Melanie M. Werst, Chaoliang Fan, Ryszard J. Gurbiel, Brian M. Hoffman, William E. Antholine, Kristene K. Surerus, James A. Fee

Publikováno v: Bioinorganic Chemistry of Copper ISBN: 9789401168779

A Mitchellian view of mitochondrial respiration is presented in Scheme I.1,2 This illustrates electron transfer from an electron rich material, NH, through quinone, Q, through Complex HI, into cytochrome c, and through Complex IV(cytochrome c oxidase

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::cf26e31762546c2875258c322884f689
https://doi.org/10.1007/978-94-011-6875-5_39

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Mode of substrate carboxyl binding to the [4Fe-4S]+ cluster of reduced aconitase as studied by 17O and 13C electron-nuclear double resonance spectroscopy

Autor: Brian M. Hoffman, Melanie M. Werst, Joshua Telser, Mark H. Emptage, Helmut Beinert, Mary Claire Kennedy

Publikováno v: Proceedings of the National Academy of Sciences. 84:8854-8858

The active form of aconitase has a diamagnetic [4Fe-4S]2+ cluster. A specific iron ion (Fea, which is lost during inactivation) is the binding site for substrate, as shown by Mössbauer spectroscopy. We have studied the mode of substrate and analogue

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4def52544957bdf7b89a85ec9471d75f
https://doi.org/10.1073/pnas.84.24.8854

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