Brian J. Hales

Louisiana State University

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Markus W. Ribbe

University of California, Irvine

Ellen E. Case

Louisiana State University

Yilin Hu

Affiliated Hospital of Nantong University

Stephen P. Cramer

Search for Extraterrestrial Intelligence

K. Rupnik

Louisiana State University

R. C. Tittsworth

Louisiana State University

Brian M. Hoffman

Northwestern University

Jason Christiansen

Virginia Tech

Morten Sørlie

Norwegian University of Life Sciences

Linda M. Cameron

Simon Fraser University

Cooperative Institutions

Louisiana State University

Northwestern University

University of California, Davis

Lawrence Berkeley National Laboratory

University of Georgia

Virginia Tech

California Institute of Technology

University of California, Irvine

Louisiana State University Agricultural Center

Massachusetts Institute of Technology

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Identification of the CO-Binding Cluster in Nitrogenase MoFe Protein by ENDOR of ⁵⁷Fe Isotopomers

Journal of the American Chemical Society (1996)

Patricia D. Christie Hong-In Lee Linda M. Cameron Brian J. Hales William H. Orme‐Johnson

The X-ray structure of the nitrogenase MoFe protein has established the organization and architecture of its multimetallic cofactors, the P-cluster (Fe8S7-8) and the FeMo-cofactor (MoFe7S9:homocitrate). Nonetheless, until recently it has not been possible to detect or characterize a substrate or inhibitor interacting with the functioning enzyme. In the present study we have used 57Fe ENDOR to study the CO-inhibited turnover states of a novel suite of 56,57Fe isotopomers of the MoFe protein, including those in which these two clusters are selectively, as well as uniformly, labeled. CO-inhibited MoFe protein exhibits two distinct EPR signals, one under low and another under high CO pressure. The 57Fe measurements, along with an earlier 13C ENDOR study of bound 13CO (Pollock, R. C.; Lee, H. I.; Cameron, L. M.; DeRose, V. J.; Hales, B. J.; Orme-Johnson, W. H.; Hoffman, B. M. J. Am. Chem. Soc. 1995, 117, 8686−8687), show that the two EPR signals arise from CO-bound FeMo-cofactor, in one case with one bound CO and in the other with two bound CO, and they further provide initial insights into the properties of the inhibitor-bound cluster.

Isotopomers

10.1021/ja961289g

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Citations (88)

ChemInform Abstract: MACROCYCLIC INCLUSION COMPLEXES. SYNTHESIS, COMPLEXATION AND X‐RAY CRYSTAL STRUCTURES OF BINUCLEAR CATION COMPLEXES OF DIPYRIDINE CROWN ETHERS

Chemischer Informationsdienst (1981)

George R. Newkome Dalip K. Kohli Frank R. Fronczek Brian J. Hales Ellen E. Case

Abstract Die Struktur und Konformation des durch 1:2‐molare Umsetzung des entsprechenden Makrocyclus mit Cu(II)‐chlorid in siedendem Methanol gebildeten Zweikernkomplexes (I) wird anhand IR‐, UV‐ und ESR‐spektroskopischer Daten diskutiert.

10.1002/chin.198111067

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Continued investigation of the various spin states of the metal clusters in the VFE-protein from Azotobacter vinelandii.

Journal of Inorganic Biochemistry (1993)

R. C. Tittsworth Carol Z. Blanchard Brian J. Hales

Azotobacter vinelandii

Azotobacteraceae

10.1016/0162-0134(93)85397-q

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Additions and Corrections

Journal of Biological Chemistry (1987)

Brian J. Hales Dieter Langosch Ellen E. Case Christy L. Cooper Sylvie Vandaele

Page 15301, right-hand column, 3rd paragraph, last sentence: The reference to Joergen et al. ( 8 ) should not have been included in this sentence since this article, in fact

Paragraph

10.1016/s0021-9258(18)61446-2

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An EPR and VTVH MCD spectroscopic investigation of the nitrogenase assembly protein NifB

JBIC Journal of Biological Inorganic Chemistry (2021)

K. Rupnik Lee A. Rettberg Kazuki Tanifuji Johannes G. Rebelein Markus W. Ribbe

Gene cluster

10.1007/s00775-021-01870-y

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Citations (1)

X-Ray Absorption Spectroscopy of Nitrogenase Mo-Fe Protein

MRS Proceedings (1993)

J. Chen J. A. Christiansen Simon J. George Roland Tittsworth Brian J. Hales

X-ray absorption spectroscopy

K-edge

X-Ray Spectroscopy

10.1557/proc-307-63

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Citations (1)

Immobilized radicals. I. Principal electron spin resonance parameters of the benzosemiquinone radical

Journal of the American Chemical Society (1975)

Brian J. Hales

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTImmobilized radicals. I. Principal electron spin resonance parameters of the benzosemiquinone radicalBrian J. HalesCite this: J. Am. Chem. Soc. 1975, 97, 21, 5993–5997Publication Date (Print):October 1, 1975Publication History Published online1 May 2002Published inissue 1 October 1975https://pubs.acs.org/doi/10.1021/ja00854a007https://doi.org/10.1021/ja00854a007research-articleACS PublicationsRequest reuse permissionsArticle Views201Altmetric-Citations86LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts

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10.1021/ja00854a007

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Citations (91)

Low-temperature MCD studies of synthetic and biological S = 3/2 [4Fe-4S]1+ centers

Journal of Inorganic Biochemistry (1989)

Michael G. Finnegan Yvonne A. Onate Brian J. Hales Robert L. Switzer M K Johnson

10.1016/0162-0134(89)84309-0

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Citations (2)

Nitrogen fixation and ammonia switch-off in the photosynthetic bacterium Rhodopseudomonas viridis

Journal of Bacteriology (1983)

K. S. Howard Brian J. Hales M. D. Socolofsky

Rhodopseudomonas viridis ATCC 19567 grows by means of nitrogen fixation in yeast extract-N2 or nitrogen-free medium when sparged with 5% CO2 and 95% N2 in the light at 30 degrees C. Acetylene reduction assays for nitrogenase activity revealed an initially high level of activity during early-logarithmic growth phase, a lower plateau during mid- to late-logarithmic phase, and a dramatic reduction of activity at the beginning of the stationary phase. When viewed by electron microscopy, nitrogen-fixing R. viridis cells appeared to be morphologically and ultrastructurally similar to cells grown on nitrogen-rich media. Whole cells prepared under reducing conditions in the dark for electron spin resonance spectroscopy yielded g4.26 and g3.66 signals characteristic of the molybdenum-iron protein of nitrogenase. During growth on N2 in the absence of fixed-nitrogen sources, the nitrogenase activity of R. viridis measured by acetylene reduction stopped rapidly in response to the addition of NH4Cl as has been observed in other Rhodospirillaceae. However, unlike the nitrogenase of Rhodopseudomonas palustris or Rhodospirillum rubrum, which recover from this treatment within 40 min, the nitrogenase activity of R. viridis was not detectable for nearly 4 h.

Rhodospirillaceae

Rhodospirillales

Rhodopseudomonas palustris

Acetylene

10.1128/jb.155.1.107-112.1983

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Citations (27)

Supposition of the origin of Signal II from random and oriented chloroplasts

Biochimica et Biophysica Acta (BBA) - Bioenergetics (1981)

Brian J. Hales Anupam Das Gupta

SIGNAL (programming language)

10.1016/0005-2728(81)90169-9

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Citations (38)