Einsle, O. (2002) Nitrogenase MoFe-Protein at 1.16 A Resolution: A Central Ligand in the FeMo-Cofactor. Science, 297 (5587). 1696-1700 doi:10.1126/science.1073877

References Listed

These are the references the publisher has listed as being connected to the article. Please check the article itself for the full list of references which may differ. Not all references are currently linkable within the Digital Library.

	Burgess, Barbara K., Lowe, David J. (1996) Mechanism of Molybdenum Nitrogenase. Chemical Reviews, 96 (7) 2983-3012 doi:10.1021/cr950055x
	Howard, James B., Rees, Douglas C. (1996) Structural Basis of Biological Nitrogen Fixation. Chemical Reviews, 96 (7) 2965-2982 doi:10.1021/cr9500545
	Not Yet Imported: Advances in Inorganic Chemistry - book-chapter : 10.1016/S0898-8838(08)60078-1 If you would like this item imported into the Digital Library, please contact us quoting Journal ID
	Not Yet Imported: Annual Review of Plant Physiology and Plant Molecular Biology - journal-article : 10.1146/annurev.arplant.52.1.269 If you would like this item imported into the Digital Library, please contact us quoting Journal ID 5389
	Not Yet Imported: Current Opinion in Chemical Biology - journal-article : 10.1016/S1367-5931(00)00132-0 If you would like this item imported into the Digital Library, please contact us quoting Journal ID 16622
	Kim, J, Rees, D. (1992) Structural models for the metal centers in the nitrogenase molybdenum-iron protein. Science, 257 (5077). 1677-1682 doi:10.1126/science.1529354
	Kirn, Jongsun, Rees, D. C. (1992) Crystallographic structure and functional implications of the nitrogenase molybdenum–iron protein from Azotobacter vinelandii. Nature, 360 (6404). 553-560 doi:10.1038/360553a0
	Chan, M., Kim, J, Rees, D. (1993) The nitrogenase FeMo-cofactor and P-cluster pair: 2.2 A resolution structures. Science, 260 (5109). 792-794 doi:10.1126/science.8484118
	Not Yet Imported: Biochemistry - journal-article : 10.1021/bi00079a006 If you would like this item imported into the Digital Library, please contact us quoting Journal ID 9134
	Not Yet Imported: ACS Symposium Series - book-chapter : 10.1021/bk-1993-0535.ch012 If you would like this item imported into the Digital Library, please contact us quoting Journal ID
	Not Yet Imported: Biochemistry - journal-article : 10.1021/bi9626665 If you would like this item imported into the Digital Library, please contact us quoting Journal ID 9134
	Mayer, Suzanne M, Lawson, David M, Gormal, Carol A, Roe, S.Mark, Smith, Barry E (1999) New insights into structure-function relationships in nitrogenase: a 1.6 Å resolution X-ray crystallographic study of Klebsiella pneumoniae MoFe-protein. Journal of Molecular Biology, 292 (4). 871-891 doi:10.1006/jmbi.1999.3107
	O. Einsle et al. unpublished data.
	(1930) LXXV.A note on the representation of crystal structure by Fourier series. The London, Edinburgh, And Dublin Philosophical Magazine And Journal Of Science, S. 7 Vol. 10 (66) 823-841 doi:10.1080/14786443009461630
	James, R. W. (1948) False detail in three-dimensional Fourier representations of crystal structures. Acta Crystallographica, 1 (3) 132-134 doi:10.1107/s0365110x48000351
	W. Cochran H. Lipson in The Determination of Crystal Structures W. L. Bragg Ed. (Cornell Univ. Press Ithaca NY ed. 3 1966).
	Materials and methods are available as supporting material on Science Online.
	Cruickshank D. W. J., Acta Crystallogr. D55, 583 (1999).
	Martinengo, Secondo, Ciani, Gianfranco, Sironi, Angelo, Heaton, Brian T., Mason, Joan (1979) Synthesis and x-ray characterization of the [M6N(.mu.-CO)9(CO)6]-(M = cobalt, rhodium) anions. A new class of metal carbonyl cluster compounds containing an interstitial nitrogen atom. Journal Of The American Chemical Society, 101 (23) 7095-7097 doi:10.1021/ja00517a067
	Thomann, H., Morgan, T. V., Jin, H., Burgmayer, S. J. N., Bare, R. E., Stiefel, E. I. (1987) Protein nitrogen coordination to the iron-molybdenum center of nitrogenase from Clostridium pasteurianum. Journal Of The American Chemical Society, 109 (25) 7913-7914 doi:10.1021/ja00259a067
	True, Anne E., McLean, Paul, Nelson, Mark J., Orme-Johnson, W. H., Hoffman, Brian M. (1990) Comparison of wild-type and nifV mutant molybdenum-iron proteins of nitrogenase from Klebsiella pneumoniae by ENDOR spectroscopy. Journal Of The American Chemical Society, 112 (2) 651-657 doi:10.1021/ja00158a024
	Not Yet Imported: Biochemistry - journal-article : 10.1021/bi980956a If you would like this item imported into the Digital Library, please contact us quoting Journal ID 9134
	R. N. F. Thorneley D. J. Lowe in Molybdenum Enzymes T. G. Spiro Ed. (Wiley-Interscience New York 1985) vol. 1 pp. 221–230.
	Not Yet Imported: Angewandte Chemie International Edition in English - journal-article : 10.1002/anie.199310621 If you would like this item imported into the Digital Library, please contact us quoting Journal ID 4535
	Stavrev, Krassimir K., Zerner, Michael C. (1996) A Theoretical Model for the Active Site of Nitrogenase. Chemistry - A European Journal, 2 (1). 83-87 doi:10.1002/chem.19960020115
	Siegbahn, Per E. M., Westerberg, Joakim, Svensson, Mats, Crabtree, Robert H. (1998) Nitrogen Fixation by Nitrogenases:  A Quantum Chemical Study. The Journal of Physical Chemistry B, 102 (9). 1615-1623 doi:10.1021/jp972207t
	Not Yet Imported: - book : 10.1002/9783527619474 If you would like this item imported into the Digital Library, please contact us quoting Book ID 9783527292127
	Logadottir, A., Nørskov, J.K. (2001) The effect of strain for N2 dissociation on Fe surfaces. Surface Science, 489 (1). 135-143 doi:10.1016/s0039-6028(01)01171-2
	This work was supported by NIH. Stanford Synchrotron Radiation Laboratory operations are funded by the U.S. Department of Energy (DOE) Office of Basic Energy Sciences and NIH. F.A.T. acknowledges the Burroughs Wellcome Fund and the Helen Hay Whitney Foundation for postdoctoral fellowships. We thank J. C. Peters J. E. Bercaw and H. B. Gray for enlightening discussions. Coordinates of the refined MoFe-protein structure have been deposited in the Protein Data Bank (accession code 1M1N).

See Also

These are possibly similar items as determined by title/reference text matching only.

	Schmid, B. (2002) Structure of a Cofactor-Deficient Nitrogenase MoFe Protein. Science, 296 (5566). 352-356 doi:10.1126/science.1070010
	Spatzal, T., Perez, K. A., Einsle, O., Howard, J. B., Rees, D. C. (2014) Ligand binding to the FeMo-cofactor: Structures of CO-bound and reactivated nitrogenase. Science, 345 (6204). 1620-1623 doi:10.1126/science.1256679
	Spatzal, T., Aksoyoglu, M., Zhang, L., Andrade, S. L. A., Schleicher, E., Weber, S., Rees, D. C., Einsle, O. (2011) Evidence for Interstitial Carbon in Nitrogenase FeMo Cofactor. Science, 334 (6058). 940 doi:10.1126/science.1214025
	Chan, M., Kim, J, Rees, D. (1993) The nitrogenase FeMo-cofactor and P-cluster pair: 2.2 A resolution structures. Science, 260 (5109). 792-794 doi:10.1126/science.8484118
	Hu, Yilin, Fay, Aaron W., Ribbe, Markus W. (2007) Molecular insights into nitrogenase FeMo cofactor insertion: the role of His 362 of the MoFe protein α subunit in FeMo cofactor incorporation. JBIC Journal of Biological Inorganic Chemistry, 12 (4) 449-460 doi:10.1007/s00775-006-0199-1
	Doray, B. (2002) Cooperation of GGAs and AP-1 in Packaging MPRs at the Trans-Golgi Network. Science, 297 (5587). 1700-1703 doi:10.1126/science.1075327
	Smith, B. E. (2002) STRUCTURE: Nitrogenase Reveals Its Inner Secrets. Science, 297 (5587). 1654-1655 doi:10.1126/science.1076659
	Hinnemann, Berit, Nørskov, Jens K. (2003) Modeling a Central Ligand in the Nitrogenase FeMo Cofactor. Journal Of The American Chemical Society, 125 (6) 1466-1467 doi:10.1021/ja029041g
	(2002) TOOLS: Tracking Protein Evolution. Science, 297 (5587). 1615 doi:10.1126/science.297.5587.1615a
	ZHAO, Ying (2005) Characterization of a FeMo cofactor-deficient MoFe protein from a nifE-deleted strain (DJ35) of Azotobacter vinelandii. Chinese Science Bulletin, 50 (20). 2305pp. doi:10.1360/982005-813
	Scott, Deborah J., May, Harold D., Newton, William E., Brigle, Kevin E., Dean, Dennis R. (1990) Role for the nitrogenase MoFe protein α-subunit in FeMo-cofactor binding and catalysis. Nature, 343 (6254). 188-190 doi:10.1038/343188a0