The Clusters of Nitrogenase: Synthetic Methodology in the Construction of Weak-Field Clusters

X-ray Crystal Structure of the Fe-Only Hydrogenase (CpI) from Clostridium pasteurianum to 1.8 Angstrom Resolution

Peters, J. W. (1998) · Science · doi:10.1126/science.282.5395.1853 · Cited by 1,891

Mechanism of Molybdenum Nitrogenase

Burgess, B. K., & Lowe, D. J. (1996) · Chemical Reviews · doi:10.1021/cr950055x · Cited by 1,854

Crystal structure of the nickel–iron hydrogenase from Desulfovibrio gigas

Volbeda, A., Charon, M.-H., Piras, C., Hatchikian, E. C., Frey, M., & Fontecilla-Camps, J. C. (1995) · Nature · doi:10.1038/373580a0 · Cited by 1,557

Structural basis of biological nitrogen fixation

Rees, D. C., Akif Tezcan, F., Haynes, C. A., Walton, M. Y., Andrade, S., Einsle, O., & Howard, J. B. (2005) · Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences · doi:10.1098/rsta.2004.1539 · Cited by 1,120

Nitrogenase MoFe-Protein at 1.16 Å Resolution: A Central Ligand in the FeMo-Cofactor

Einsle, O., Tezcan, F. A., Andrade, S. L. A., Schmid, B., Yoshida, M., Howard, J. B., & Rees, D. C. (2002) · Science · doi:10.1126/science.1073877 · Cited by 1,093

Structural Basis of Biological Nitrogen Fixation

Howard, J. B., & Rees, D. C. (1996) · Chemical Reviews · doi:10.1021/cr9500545 · Cited by 1,044

Structure–function relationships of alternative nitrogenases

Eady, R. R. (1996) · Chemical Reviews · doi:10.1021/cr950057h · Cited by 877

Metal-Ligand Multiple Bonds

Maatta, E. (1989) · Organometallics · doi:10.1021/om00114a601 · Cited by 667

The Art and Science of Total Synthesis at the Dawn of the Twenty-First Century

Nicolaou, K. C., Vourloumis, D., Winssinger, N., & Baran, P. S. (2000) · Angewandte Chemie International Edition · doi:10.1002/(sici)1521-3773(20000103)39:1<44::aid-anie44>3.0.co;2-l · Cited by 626

Crystallographic structure and functional implications of the nitrogenase molybdenum–iron protein from Azotobacter vinelandii

Kirn, J., & Rees, D. C. (1992) · Nature · doi:10.1038/360553a0 · Cited by 612

Isolation of an iron-molybdenum cofactor from nitrogenase

Shah, V. K., & Brill, W. J. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.8.3249 · Cited by 593

Transition Metal Thiometalates: Properties and Significance in Complex and Bioinorganic Chemistry

Müller, A., Diemann, E., Jostes, R., & Bögge, H. (1981) · Angewandte Chemie International Edition in English · doi:10.1002/anie.198109341 · Cited by 585

Crystal Structure of a Carbon Monoxide Dehydrogenase Reveals a [Ni-4Fe-5S] Cluster

Dobbek, H., Svetlitchnyi, V., Gremer, L., Huber, R., & Meyer, O. (2001) · Science · doi:10.1126/science.1061500 · Cited by 570

Synthetic Analogues of the Active Sites of Iron−Sulfur Proteins

Venkateswara Rao, P., & Holm, R. H. (2004) · Chemical Reviews · doi:10.1021/cr020615+ · Cited by 541

A Ni-Fe-Cu Center in a Bifunctional Carbon Monoxide Dehydrogenase/ Acetyl-CoA Synthase

Doukov, T. I., Iverson, T. M., Seravalli, J., Ragsdale, S. W., & Drennan, C. L. (2002) · Science · doi:10.1126/science.1075843 · Cited by 529

Redox-Dependent Structural Changes in the Nitrogenase P-Cluster,

Peters, J. W., Stowell, M. H. B., Soltis, S. M., Finnegan, M. G., Johnson, M. K., & Rees, D. C. (1997) · Biochemistry · doi:10.1021/bi9626665 · Cited by 481

The Nitrogenase FeMo-Cofactor and P-Cluster pair: 2.2 Å Resolution Structures

Chan, M. K., Kim, J., & Rees, D. C. (1993) · Science · doi:10.1126/science.8484118 · Cited by 444

Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] clusters in closed and open α subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase

Darnault, C., Volbeda, A., Kim, E. J., Legrand, P., Vernède, X., Lindahl, P. A., & Fontecilla-Camps, J. C. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb912 · Cited by 433

A novel FeS cluster in Fe-only hydrogenases

Nicolet, Y., Lemon, B. J., Fontecilla-Camps, J. C., & Peters, J. W. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01536-4 · Cited by 417

Catalysis at a dinuclear [CuSMo(O)OH] cluster in a CO dehydrogenase resolved at 1.1-Å resolution

Dobbek, H., Gremer, L., Kiefersauer, R., Huber, R., & Meyer, O. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.212640899 · Cited by 386

The iron-molybdenum cofactor of nitrogenase

Burgess, B. K. (1990) · Chemical Reviews · doi:10.1021/cr00106a002 · Cited by 351

Sulfite Reductase Structure at 1.6 Å: Evolution and Catalysis for Reduction of Inorganic Anions

Crane, B. R., Siegel, L. M., & Getzoff, E. D. (1995) · Science · doi:10.1126/science.270.5233.59 · Cited by 345

Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase

Drennan, C. L., Heo, J., Sintchak, M. D., Schreiter, E., & Ludden, P. W. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.211429998 · Cited by 322

Current status of structure function relationships of vanadium nitrogenase

Eady, R. (2003) · Coordination Chemistry Reviews · doi:10.1016/s0010-8545(02)00248-5 · Cited by 285

Synthetic analogs of the active sites of iron-sulfur proteins. II. Synthesis and structure of the tetra[mercapto-.mu.3-sulfido-iron] clusters, [Fe4S4(SR)4]2-

Averill, B. A., Herskovitz, T., Holm, R. H., & Ibers, J. A. (1973) · Journal of the American Chemical Society · doi:10.1021/ja00792a013 · Cited by 277

New insights into structure-function relationships in nitrogenase: a 1.6 Å resolution X-ray crystallographic study of Klebsiella pneumoniae MoFe-protein

Mayer, S. M., Lawson, D. M., Gormal, C. A., Roe, S. M., & Smith, B. E. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3107 · Cited by 270

Centenary Lecture. Metal clusters in biology: quest for a synthetic representation of the catalytic site of nitrogenase

Holm, R. H. (1981) · Chemical Society Reviews · doi:10.1039/cs9811000455 · Cited by 233

Formation of iron–sulfur clusters in bacteria: an emerging field in bioinorganic chemistry

Frazzon, J. (2003) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(03)00021-8 · Cited by 220

[NiFe] hydrogenase from Desulfovibrio desulfuricans ATCC 27774: gene sequencing, three-dimensional structure determination and refinement at 1.8 Å and modelling studies of its interaction with the tetrahaem cytochrome c 3

Matias, P. M., Soares, C. M., Saraiva, L. M., Coelho, R., Morais, J., Le Gall, J., & Carrondo, M. A. (2001) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s007750000167 · Cited by 215

Structure and Properties of a Synthetic Analogue of Bacterial Iron-Sulfur Proteins

Herskovitz, T., Averill, B. A., Holm, R. H., Ibers, J. A., Phillips, W. D., & Weiher, J. F. (1972) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.69.9.2437 · Cited by 212

The molybdenum site of nitrogenase. 2. A comparative study of molybdenum-iron proteins and the iron-molybdenum cofactor by x-ray absorption spectroscopy

Cramer, S. P., Gillum, W. O., Hodgson, K. O., Mortenson, L. E., Stiefel, E. I., Chisnell, J. R., Brill, W. J., & Shah, V. K. (1978) · Journal of the American Chemical Society · doi:10.1021/ja00480a027 · Cited by 195

Structure of a Cofactor-Deficient Nitrogenase MoFe Protein

Schmid, B., Ribbe, M. W., Einsle, O., Yoshida, M., Thomas, L. M., Dean, D. R., Rees, D. C., & Burgess, B. K. (2002) · Science · doi:10.1126/science.1070010 · Cited by 186

Use of preassembled iron/sulfur and iron/molybdenum/sulfur clusters in the stepwise synthesis of potential analogs for the Fe/Mo/S site in nitrogenase

Coucouvanis, D. (1991) · Accounts of Chemical Research · doi:10.1021/ar00001a001 · Cited by 181

Synthetic approaches to the active sites of iron-sulfur proteins

Holm, R. H. (1977) · Accounts of Chemical Research · doi:10.1021/ar50120a001 · Cited by 175

Atomically defined mechanism for proton transfer to a buried redox centre in a protein

Chen, K., Hirst, J., Camba, R., Bonagura, C. A., Stout, C. D., Burgess, B. K., & Armstrong, F. A. (2000) · Nature · doi:10.1038/35015610 · Cited by 158

Definition of reaction sequences resulting in self-assembly of [Fe4S4(SR)4]2- clusters from simple reactants

Hagen, K. S., Reynolds, J. G., & Holm, R. H. (1981) · Journal of the American Chemical Society · doi:10.1021/ja00404a013 · Cited by 151

M ECHANISTIC F EATURES OF THE M O -C ONTAINING N ITROGENASE

Christiansen, J., Dean, D. R., & Seefeldt, L. C. (2001) · Annual Review of Plant Physiology and Plant Molecular Biology · doi:10.1146/annurev.arplant.52.1.269 · Cited by 143

Probing the Catalytic Mechanism of Sulfite Reductase by X-ray Crystallography: Structures of the Escherichia coli Hemoprotein in Complex with Substrates, Inhibitors, Intermediates, and Products,

Crane, B. R., Siegel, L. M., & Getzoff, E. D. (1997) · Biochemistry · doi:10.1021/bi971066i · Cited by 125

Polycubane Clusters: Synthesis of [Fe4S4(PR3)4]1+,0 (R = But, Cy, Pri) and [Fe4S4]0 Core Aggregation upon Loss of Phosphine

Goh, C., Segal, B. M., Huang, J., Long, J. R., & Holm, R. H. (1996) · Journal of the American Chemical Society · doi:10.1021/ja9620200 · Cited by 111

Synthesis of a Molecular Mo2Fe6S9 Cluster with the Topology of the PN Cluster of Nitrogenase by Rearrangement of an Edge-Bridged Mo2Fe6S8 Double Cubane

Zhang, Y., & Holm, R. H. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0214633 · Cited by 110

Heterometal Cubane-Type MFe3S4Clusters (M = Mo, V) Trigonally Symmetrized with Hydrotris(pyrazolyl)borate(1−) and Tris(pyrazolyl)methanesulfonate(1−) Capping Ligands

Fomitchev, D. V., McLauchlan, C. C., & Holm, R. H. (2002) · Inorganic Chemistry · doi:10.1021/ic011106d · Cited by 110

Synthesis of the P-Cluster Inorganic Core of Nitrogenases

Ohki, Y., Sunada, Y., Honda, M., Katada, M., & Tatsumi, K. (2003) · Journal of the American Chemical Society · doi:10.1021/ja029383m · Cited by 107

The vanadium-iron protein of vanadium nitrogenase from Azotobacter chroococcum contains an iron-vanadium cofactor

Smith, B. E., Eady, R. R., Lowe, D. J., & Gormal, C. A. (1988) · Biochemical Journal · doi:10.1042/bj2500299 · Cited by 101

The Fe-only nitrogenase from Rhodobacter capsulatus: identification of the cofactor, an unusual, high-nuclearity iron-sulfur cluster, by Fe K-edge EXAFS and 57Fe Mössbauer spectroscopy

Krahn, E., Weiss, B., Kröckel, M., Groppe, J., Henkel, G., Cramer, S. P., TRAUTWEIN, A. X., Schneider, K., & Müller, A. (2001) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s007750100263 · Cited by 100

Speculative synthetic chemistry and the nitrogenase problem

Lee, S. C., & Holm, R. H. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0630028100 · Cited by 97

The Interstitial Atom of the Nitrogenase FeMo-Cofactor: ENDOR and ESEEM Show It Is Not an Exchangeable Nitrogen

Lee, H.-I., Benton, P. M. C., Laryukhin, M., Igarashi, R. Y., Dean, D. R., Seefeldt, L. C., & Hoffman, B. M. (2003) · Journal of the American Chemical Society · doi:10.1021/ja034383n · Cited by 95

Structural characterization of [AsPh4]+[Fe4(NO)7(.mu.3-S)3]-. Stereochemical and bonding relationship of the Roussin black monoanion with the red ethyl ester, Fe2(NO)4(.mu.2-SC2H5)2, and Fe4(NO)4(.mu.3-S)4

CHU, C. T. ‐., & Dahl, L. F. (1977) · Inorganic Chemistry · doi:10.1021/ic50178a052 · Cited by 69

Vanadium−Iron−Sulfur Clusters Containing the Cubane-type [VFe3S4] Core Unit: Synthesis of a Cluster with the Topology of the PN Cluster of Nitrogenase

Zuo, J., Zhou, H.-C. “., & Holm, R. H. (2003) · Inorganic Chemistry · doi:10.1021/ic0301369 · Cited by 64

Synthesis and Characterization of Sulfur-Voided Cubanes. Structural Analogues for the MoFe3S3 Subunit in the Nitrogenase Cofactor

Coucouvanis, D., Han, J., & Moon, N. (2001) · Journal of the American Chemical Society · doi:10.1021/ja0110832 · Cited by 60

Chemical approaches to bridged biological metal assemblies

Holm, R. H. (1995) · Pure and Applied Chemistry · doi:10.1351/pac199567020217 · Cited by 60

Molybdenum−Iron Sulfide-Bridged Double Cubanes

Huang, J., Mukerjee, S., Segal, B. M., Akashi, H., Zhou, J., & Holm, R. H. (1997) · Journal of the American Chemical Society · doi:10.1021/ja971401q · Cited by 56

Iron−Arylimide Clusters [Fem(NAr)nCl4]2- (m, n = 2, 2; 3, 4; 4, 4) from a Ferric Amide Precursor: Synthesis, Characterization, and Comparison to Fe−S Chemistry

Duncan, J. S., Nazif, T. M., Verma, A. K., & Lee, S. C. (2003) · Inorganic Chemistry · doi:10.1021/ic025825j · Cited by 54

Metal Substitution in the Active Site of Nitrogenase MFe7S9 (M = Mo4+, V3+, Fe3+)

Lovell, T., Torres, R. A., Han, W., Liu, T., Case, D. A., & Noodleman, L. (2002) · Inorganic Chemistry · doi:10.1021/ic020474u · Cited by 54

Reduced Mono-, Di-, and Tetracubane-Type Clusters Containing the [MoFe3S4]2+ Core Stabilized by Tertiary Phosphine Ligation

Osterloh, F. E., Segal, B. M., Achim, C., & Holm, R. H. (2000) · Inorganic Chemistry · doi:10.1021/ic991016x · Cited by 49

Synthesis and proton magnetic resonance properties of Fe3Ms4(M = Mo or W) cubane-like cluster dimers

Christou, G., & Garner, C. D. (1980) · Journal of the Chemical Society Dalton Transactions · doi:10.1039/dt9800002354 · Cited by 47

Synthetic Analogs for the MoFe3S3 Subunit of the Nitrogenase Cofactor: Structural Features Associated with the Total Number of Valence Electrons and the Possible Role of M−M and Multiple M−S Bonding in the Function of Nitrogenase

Han, J., Beck, K., Ockwig, N. W., & Coucouvanis, D. (1999) · Journal of the American Chemical Society · doi:10.1021/ja991880o · Cited by 46

Structural basis of biological nitrogen fixation

Rees, D. C., Akif Tezcan, F., Haynes, C. A., Walton, M. Y., Andrade, S., Einsle, O., & Howard, J. B. (2005) · Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences · doi:10.1098/rsta.2004.1539 · Cited by 1,120