NDLI: How nitrogenase shakes--initial information about P-cluster and FeMo-cofactor normal modes from nuclear resonance vibrational spectroscopy (NRVS).

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How nitrogenase shakes--initial information about P-cluster and FeMo-cofactor normal modes from nuclear resonance vibrational spectroscopy (NRVS).

Content Provider	Semantic Scholar
Author	Xiao, Yuming Fisher, Karl B. Smith, Matt C. Newton, William E. Case, David A. George, Simon J. Wang, Hongxin Sturhahn, Wolfgang Alp, Ercan E. Zhao, Jiyong Yoda, Yoshitaka Cramer, Stephen P.
Copyright Year	2006
Abstract	Nitrogenase catalyzes a reaction critical for life, the reduction of N(2) to 2NH(3), yet we still know relatively little about its catalytic mechanism. We have used the synchrotron technique of (57)Fe nuclear resonance vibrational spectroscopy (NRVS) to study the dynamics of the Fe-S clusters in this enzyme. The catalytic site FeMo-cofactor exhibits a strong signal near 190 cm(-)(1), where conventional Fe-S clusters have weak NRVS. This intensity is ascribed to cluster breathing modes whose frequency is raised by an interstitial atom. A variety of Fe-S stretching modes are also observed between 250 and 400 cm(-)(1). This work is the first spectroscopic information about the vibrational modes of the intact nitrogenase FeMo-cofactor and P-cluster.
Starting Page	97
Ending Page	105
Page Count	9
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://chemgroups.ucdavis.edu/~cramer/Publications_pdf/cramer_174.pdf
PubMed reference number	16756317v1
Volume Number	128
Issue Number	23
Journal	Journal of the American Chemical Society
Language	English
Access Restriction	Open
Subject Keyword	Catalytic Domain Exhibits as Topic Iron Magnetic Resonance Imaging Synchrotrons Tremor chemical cofactor vanadium-iron nitrogenase complex
Content Type	Text
Resource Type	Article

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