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CRYSTAL-STRUCTURE OF METHYL COENZYME M-REDUCTASE - THE KEY ENZYME OF BIOLOGICAL METHANE FORMATION
Authors: ERMLER U GRABARSE W SHIMA S GOUBEAUD M THAUER RK
Citation: U. Ermler et al., CRYSTAL-STRUCTURE OF METHYL COENZYME M-REDUCTASE - THE KEY ENZYME OF BIOLOGICAL METHANE FORMATION, Science, 278(5342), 1997, pp. 1457-1462
CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF METHYL-COENZYME-M REDUCTASE FROM METHANOBACTERIUM-THERMOAUTOTROPHICUM
Authors: SHIMA S GOUBEAUD M VINZENZ D THAUER RK ERMLER U
Citation: S. Shima et al., CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF METHYL-COENZYME-M REDUCTASE FROM METHANOBACTERIUM-THERMOAUTOTROPHICUM, Journal of Biochemistry, 121(5), 1997, pp. 829-830
PURIFIED METHYL-COENZYME-M REDUCTASE IS ACTIVATED WHEN THE ENZYME-BOUND COENZYME F430 IS REDUCED TO THE NICKEL(I) OXIDATION-STATE BY TITANIUM(III) CITRATE
Authors: GOUBEAUD M SCHREINER G THAUER RK
Citation: M. Goubeaud et al., PURIFIED METHYL-COENZYME-M REDUCTASE IS ACTIVATED WHEN THE ENZYME-BOUND COENZYME F430 IS REDUCED TO THE NICKEL(I) OXIDATION-STATE BY TITANIUM(III) CITRATE, European journal of biochemistry, 243(1-2), 1997, pp. 110-114
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