Emeritus Prof. Ian Dance

 

Ian Gordon Dance

M.Sc. Syd., Ph.D. Manc., CChem, FRACI, FAA
Emeritus Professor
E-mail: i.dance@unsw.edu.au

BIOGRAPHICAL DETAILS

Born 1940. Ph.D. Manchester University. Assistant Professor, University of Wisconsin, Madison, Wis., USA, 1968-1974. At UNSW: Lecturer (1975), Senior Lecturer (1976), Associate Professor (1981), Professor of Inorganic Chemistry (1986), Head of School of Chemistry (1990-1993), Faculty of Science Professor (2000), Emeritus Professor (2002). Royal Society of Chemistry Lecturer for Australia and New Zealand 1993/4; Panel member of the Australian Research Council 1995-1997; Burrows Lecturer, RACI, 1996. Fellow of the Australian Academy 1997. Stranks Lecture (Melbourne) 1997; Albright and Wilson lecturer, University of Warwick, July 1999; 3M lecturer, University of Western Ontario, May 2000; Dwyer Lecturer (UNSW) 2002. David Craig Medal of the Australian Academy of Science (2011).

RESEARCH INTERESTS

My research programs have been in four areas:

  1. Metal-thiolate and metal-chalcogenide cluster chemistry.
  2. Gas phase inorganic chemistry.
  3. Crystal supramolecular chemistry and inorganic supramolecular chemistry.
  4. The mechanism of biological nitrogen fixation.

Since formally retiring from the University of New South Wales in 2002 my principal research project is the investigation of the mechanism of the enzyme nitrogenase, using density functional simulations of the structures of intermediates and of reaction trajectories. In 2001 further significant information was revealed about the structure of the FeMo-cofactor (FeMo-co) which is the active catalytic site for the hydrogenation of N2 to NH3, permitting me further insight into the coordination chemistry involved. FeMo-co is an unprecedented Fe7MoS9N(homocitrate) metal chalcogenide cluster. Also at this time key experimental information about the effects of mutation of residues around FeMo-co started to be published, allowing me to focus on specific sites and volumes for the chemical steps which comprise the mechanism. I have developed methodologies for incorporating the complex electronic structure of FeMo-co in simulations of reaction profiles. Detailed explorations of the coordination chemistry of FeMo-co with H2, H, and N2, using density functional calculations and simulations, have defined the fundamental principles for this unprecedented and enigmatic chemistry, and indicated the most probable mechanistic pathways for the catalysis. In 2008 I published a detailed 21 step chemical mechanism for the enzymatic catalysis of N2 fixation to NH3 (together with predictions of the importance of H-atom tunneling). Current research is focusing on the mechanism of the reaction D2 + 2H+ + 2e- → 2HD, catalysed by FeMo-co only when N2 is present: an understanding of the mechanism of this reaction is crucial to confirmation of the chemical mechanism of nitrogen fixation. I am also exploring mechanisms for the recent experimental finding that vanadium nitrogenase converts CO to hydrocarbons.

PUBLICATIONS on the mechanism of biological nitrogen fixation

286.  Survey of the geometric and electronic structures of the key hydrogenated forms of FeMo-co, the active site of the enzyme nitrogenase: principles of the mechanistically significant coordination chemistry. Ian Dance, Inorganics 7, 8 (2019), doi:10.3390/inorganics7010008

285.  How feasible is the reversible S-dissociation mechanism for the activation of FeMo-co, the catalytic site of nitrogenase? Ian Dance, Dalton Trans 48, 1251-1262  (2019), doi: 10.1039/c8dt04531c

284.  What is the role of the isolated small water pool near FeMo‐co, the active site of nitrogenase? Ian Dance, The FEBS Journal, 285, 2972-2986 (2018), doi:10.1111/febs.14519

283.  Evaluations of the Accuracies of DMol3 Density Functionals for Calculations of Experimental Binding Enthalpies of N2, CO, H2, C2H2 at Catalytic Metal Sites, Ian Dance, Molecular Simulations, 44, 568-581 (2018), doi.org/10.1080/08927022.2017.1413711

282   New insights into the reaction capabilities of His195 adjacent to the active site of nitrogenase. Ian Dance, Journal of Inorganic Biochemistry, 169, 32-43 (2017), DOI: 10.1016/j.jinorgbio.2017.01.005.

281.  Mechanisms of the S/CO/Se interchange reactions at FeMo-co, the active site cluster of nitrogenase. Ian Dance, Dalton Transactions, 45, 14285-14300 (2016), DOI: 10.1039/C6DT03159E.

280.  The pathway for serial proton supply to the active site of nitrogenase: enhanced density functional modeling of the Grotthuss mechanism.  Ian Dance, Dalton Transactions, 44, 18167-18186 (2015), DOI: 10.1039/C5DT03223G

279.  Misconception of reductive elimination of H2, in the context of the mechanism of nitrogenase.  Ian Dance, Dalton Transactions, 44, 9027-9037 (2015)  DOI: 10.1039/C5DT00771B

276.  A Unified Chemical Mechanism for Hydrogenation Reactions Catalysed by Nitrogenase.  Ian Dance, in Bioinspired Catalysis. Metal-Sulfur Complexes, editors Philippe Schollhammer, Wolfgang Weigand, Wiley VCH, chapter 10, 249-288 (2015)  DOI: 10.1039/C4SC03223C.

275.  Activation of N2, the Enzymatic Way. Ian Dance,  Zeitschrift für anorganische und allgemeine Chemie, 641, 91-99 (2015)  DOI: 10.1002/zaac.201400120.

272.  A molecular pathway for the egress of ammonia produced by nitrogenase.  Ian Dance, Sci Rep3, 3237 (2013) DOI; 10.1038/srep03237.

271.  The Stereochemistry and Dynamics of the Introduction of Hydrogen Atoms onto FeMo-co, the Active Site of Nitrogenase, Ian Dance, Inorg. Chem., 22, 13068-13077 (2013) DOI: 10.1021/ic401818k

270.  Nitrogenase: a general hydrogenator of small molecules.  Ian Dance, Chem. Commun., 49, 10893-10907 (2013) DOI 10.1039/c3cc46864j.

269.  The controlled relay of multiple protons required at the active site of nitrogenase.  Ian Dance, Dalton Transactions, 41, 7647-7659 (2012). doi: 10.1039/C2DT30518F

268.  Ramifications of C-centering rather than N-centering of the active site FeMo-co of the enzyme nitrogenase.  Ian Dance, Dalton Transactions, 41, 4859-4865 (2012). DOI: 10.1039/c2dt00049k.

267.  Calculated vibrational frequencies for FeMo-co, the active site of nitrogenase, bearing hydrogen atoms and carbon monoxide.  Ian Dance, Dalton Transactions, 40, 6480-6489 (2011). doi 10.1039/C1DT10505A.

266.  How does vanadium nitrogenase reduce CO to hydrocarbons?  Ian Dance, Dalton Transactions, 40, 5516-5527 (2011). doi: 10.1039/C1DT10240K

265.  The Electronic Dimensions of FeMo-co, the Active Site of Nitrogenase, and its Catalytic Intermediates, Ian Dance, Inorg. Chem., 50, 178-192 (2011). doi: 10.1021/ic1015884

262.  Mimicking Nitrogenase, Ian Dance, Dalton Transactions, 39, 2972-2983 (2010). doi: 10.1039/B922606K

259.  A pragmatic method for location of transition states and calculation of reaction paths.  Ian Dance, Molecular Simulations, 34, 923-929 (2008); 37, 257 (2011).

258.  The chemical mechanism of nitrogenase:  hydrogen tunneling and further aspects of the intramolecular mechanism for hydrogenation of h2-N2 on FeMo-co to NH3.  Ian Dance, Dalton Transactions, 5992-5998 (2008). doi: 10.1039/B806103C

257.  The chemical mechanism of nitrogenase:  calculated details of the intramolecular mechanism for hydrogenation of h2-N2 on FeMo-co to NH3.  Ian Dance, Dalton Transactions, 5977-5991 (2008). doi: 10.1039/B806100A

255.  Elucidating the Coordination Chemistry and Mechanism of Biological Nitrogen Fixation, Ian Dance, Chemistry, an Asian Journal, 2, 936-946 (2007).  An invited Focus Review. doi: 10.1002/asia.200700131

254.  The mechanistically significant coordination chemistry of dinitrogen at FeMo-co, the catalytic site of nitrogenase,  Ian Dance, J. Am. Chem. Soc., 129, 1076-1088 (2007).

251.  The correlation of redox potential, HOMO energy, and oxidation state in metal clusters, and its application to determination of the redox level of the FeMo-co active site cluster of nitrogenase, Ian  Dance, Inorg. Chem. 45, 5084-5091 (2006).

250.  Mechanistic significance of the preparatory migration of hydrogen atoms around the FeMoco active site of nitrogenase,  Ian Dance, Biochemistry, 45, 6328-6340 (2006).

246.  The hydrogen chemistry of the FeMo-co active site of nitrogenase.  Ian Dance, J. Am. Chem. Soc., 127, 10925-10942 (2005).

240.  The mechanism of nitrogenase.   Computed details of the site and geometry of binding of alkyne and alkene substrates and intermediates.   Ian Dance, J. Am. Chem. Soc. 126, 11852-11863 (2004).

239.  Localization of a Catalytic Intermediate Bound to FeMo-cofactor of Nitrogenase.   Robert Y. Igarashi, Patricia C. Dos Santos, Walter G. Niehaus, Ian G. Dance, Dennis R. Dean, and Lance C. Seefeldt.  J. Biol. Chem. 279, 34770-34775 (2004).

238.  Substrate Interactions with Nitrogenase: Fe versus Mo.  Lance C. Seefeldt, Ian G. Dance, and Dennis R. Dean, Biochemistry, 43, 1401-1409 (2004).

230.  The consequences of an interstitial N atom in the FeMo cofactor of nitrogenase, Ian Dance,  Chemical Commun, 324–325 (2003).

169.  Understanding structure and reactivity of new fundamental inorganic molecules:  metal sulfides, metallocarbohedrenes, and nitrogenase.  Ian Dance,  Chemical Communications, 523-530, 1998.

156.  Calculated Details of a Mechanism for Conversion of N2 to NH3 at the FeMo Cluster of Nitrogenase, Ian Dance, J. Chem. Soc., Chem. Comm., 165-166, 1997.

152.  Theoretical Investigations of the Mechanism of Biological Nitrogen Fixation at the FeMo Cluster Site, Ian Dance, J. Biol. Inorg. Chem., 1, 581-586 (1996).

126.  The Binding and Reduction of Dinitrogen at an Fe4 Face of the FeMo Cluster of Nitrogenase,  I.G. Dance,  Aust. J. Chem., 47, 979-990, 1994.

Full publication list (PDF file).