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Belt-Sulfur Mobilization as a Crucial Mechanistic Feature Shared between the Vanadium and Molybdenum Nitrogenases
Chi Chung Lee1, Kuntal Chatterjee2, Junko Yano2
1Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697- 3900, USA.
Abstract:
Nitrogenase catalyzes the reduction of N2 to NH3 at its active-site cofactor. Recent studies of the 'conventional' Mo-nitrogenase suggest a plausible involvement of all cofactor belt-S sites in catalysis. Here, we use analytical, enzymatic and spectroscopic methods to demonstrate the same dynamic belt-S mobilization by the 'alternative' V-nitrogenase during catalysis. Our results point to belt-S turnover as a common catalytic feature of the homologous Mo- and V-nitrogenases while identifying an activated, but N2-free conformation of the V-nitrogenase that bears great potential for facilitating future mechanistic explorations of the intriguing nitrogenase enzyme.
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