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Enzymes / Cofactors / Metal dithiolene complex / Transition metal oxo complex / Molybdenum / Cluster chemistry / Sulfite oxidase / Ferredoxin / Coordination complex / Chemistry / Transition metals / Iron-sulfur proteins


Document Date: 2004-06-03 12:09:36

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City

Washington / D.C. / New York / /

Company

Hodgson A. E. / Academic Press / NCH / Second Ed. Wolfe Publishing / K. F. Miller A. E. / ACS / Ligand / Engineering Co. / andModel Systems / Chemistry (R. B. King Ed.) John Wiley and Sons / /

Country

United States / United Kingdom / /

Facility

IV complex / terminal Mo / /

IndustryTerm

active site / molybdenum site / sulfido mono pterin-dithiolene site / transition metal sulfur complexes / metal / chemical reactivity / chemical synthesis / excess energy / metal sphere / low energy / inorganic systems / nitrogenase site / metal coordination sphere / metal-based electron transfer / high energy states / metal coordination spheres / metal oxidation state / excess reaction energy / metal centers / polynuclear metal sulfide groupings / polynuclear metal sulfide clusters / high energy intermediates / mono 0x0 sulfhydryl site / lower energy / negative free energy change / mononuclear metal site / lowest energy / multisulhr transition metal systems / metallo active site / chemical preparation / energy / /

Person

J. M. Berg / Prince / Marcel Dekker / Clinton Townshb / Molybdenum Enzymes / Mo(V) Sulfido Dithiolene / Edward I. Stiefel Exxon / J. C. Boyington / V / /

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Position

Archer / Rt / D. J. / /

ProvinceOrState

Missouri / New York / /

PublishedMedium

Pure and Applied Chemistry / /

Technology

x-ray / /

SocialTag