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

Yuming Xiao; Karl Fisher; Matt C Smith; William E Newton; David A Case; Simon J George; Hongxin Wang; Wolfgang Sturhahn; Ercan E Alp; Jiyong Zhao; Yoshitaka Yoda; Stephen P Cramer

doi:10.1021/ja0603655

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

Yuming Xiao, Karl Fisher, Matt C Smith, William E Newton, David A Case, Simon J George, Hongxin Wang, Wolfgang Sturhahn, Ercan E Alp, Jiyong Zhao, Yoshitaka Yoda, Stephen P Cramer

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	7608-7612
Number of pages	4
Journal	Journal of the American Chemical Society
Volume	128
Issue number	23
DOIs	https://doi.org/10.1021/ja0603655
Publication status	Published - 14 Jun 2006

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Xiao, Y., Fisher, K., Smith, M. C., Newton, W. E., Case, D. A., George, S. J., Wang, H., Sturhahn, W., Alp, E. E., Zhao, J., Yoda, Y., & Cramer, S. P. (2006). How nitrogenase shakes--initial information about P-cluster and FeMo-cofactor normal modes from nuclear resonance vibrational spectroscopy (NRVS). Journal of the American Chemical Society, 128(23), 7608-7612. https://doi.org/10.1021/ja0603655

@article{1133e09d0d4648789db6402e8f39f375,

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

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.",

author = "Yuming Xiao and Karl Fisher and Smith, {Matt C} and Newton, {William E} and Case, {David A} and George, {Simon J} and Hongxin Wang and Wolfgang Sturhahn and Alp, {Ercan E} and Jiyong Zhao and Yoshitaka Yoda and Cramer, {Stephen P}",

note = "DK-37255, NIDDK NIH HHS, United StatesGM-39914, NIGMS NIH HHS, United StatesGM-44380, NIGMS NIH HHS, United StatesGM-65440, NIGMS NIH HHS, United StatesR01 EB001962, NIBIB NIH HHS, United StatesR01 EB001962-15, NIBIB NIH HHS, United StatesR01 GM065440, NIGMS NIH HHS, United StatesR01 GM065440-08W1, NIGMS NIH HHS, United States",

year = "2006",

month = jun,

day = "14",

doi = "10.1021/ja0603655",

language = "English",

volume = "128",

pages = "7608--7612",

journal = "Journal of the American Chemical Society",

issn = "1520-5126",

publisher = "American Chemical Society",

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Xiao, Y, Fisher, K, Smith, MC, Newton, WE, Case, DA, George, SJ, Wang, H, Sturhahn, W, Alp, EE, Zhao, J, Yoda, Y & Cramer, SP 2006, 'How nitrogenase shakes--initial information about P-cluster and FeMo-cofactor normal modes from nuclear resonance vibrational spectroscopy (NRVS).', Journal of the American Chemical Society, vol. 128, no. 23, pp. 7608-7612. https://doi.org/10.1021/ja0603655

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T1 - How nitrogenase shakes--initial information about P-cluster and FeMo-cofactor normal modes from nuclear resonance vibrational spectroscopy (NRVS).

AU - Xiao, Yuming

AU - Fisher, Karl

AU - Smith, Matt C

AU - Newton, William E

AU - Case, David A

AU - George, Simon J

AU - Wang, Hongxin

AU - Sturhahn, Wolfgang

AU - Alp, Ercan E

AU - Zhao, Jiyong

AU - Yoda, Yoshitaka

AU - Cramer, Stephen P

N1 - DK-37255, NIDDK NIH HHS, United StatesGM-39914, NIGMS NIH HHS, United StatesGM-44380, NIGMS NIH HHS, United StatesGM-65440, NIGMS NIH HHS, United StatesR01 EB001962, NIBIB NIH HHS, United StatesR01 EB001962-15, NIBIB NIH HHS, United StatesR01 GM065440, NIGMS NIH HHS, United StatesR01 GM065440-08W1, NIGMS NIH HHS, United States

PY - 2006/6/14

Y1 - 2006/6/14

N2 - 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.

AB - 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.

U2 - 10.1021/ja0603655

DO - 10.1021/ja0603655

M3 - Article

C2 - 16756317

SN - 1520-5126

VL - 128

SP - 7608

EP - 7612

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 23

ER -

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

Abstract

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