Time-Resolved Binding of Carbon Monoxide to Nitrogenase Monitored by Stopped-Flow Infrared Spectroscopy

George, Simon J.; Ashby, G. A.; Wharton, Christopher W.; Thorneley, R. N. F.

doi:10.1021/ja971088s

Cited by 115 publications

(184 citation statements)

References 20 publications

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“…Gas or solute triggers using stop-flow mixing approaches are limited by mixing times and therefore generally limited to the ms time domain. However, stop-flow mixing was used productively in conjunction with a conventional FTIR instrument set up in an anaerobic glove box by George et al (1997) for a series of studies of CO binding to the nitrogenase enzyme. One way to take time resolution into the ms domain in solute concentration triggered experiments is the use of caged starting materials which are released in response to a light pulse, in conjunction with time-resolved IR step-scan methods (Cheng et al 2002).…”

Section: (B) Gas Exchange or Solute Exchange As A Reaction Triggermentioning

confidence: 99%

Triggered infrared spectroscopy for investigating metalloprotein chemistry

Vincent

2010

Phil. Trans. R. Soc. A.

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Recent developments in infrared (IR) spectroscopic time resolution, sensitivity and sample manipulation make this technique a powerful addition to the suite of complementary approaches for the study of time-resolved chemistry at metal centres within proteins. Application of IR spectroscopy to proteins has often targeted the amide bands as probes for gross structural change. This article focuses on the possibilities arising from recent IR technical developments for studies that monitor localized vibrational oscillators in proteins-native or exogenous ligands such as NO, CO, SCN − or CN − , or genetically or chemically introduced probes with IR-active vibrations. These report on the electronic and coordination state of metals, the kinetics, intermediates and reaction pathways of ligand release, hydrogen-bonding interactions between the protein and IR probe, and the electrostatic character of sites in a protein. Metalloprotein reactions can be triggered by light/dark transitions, an electrochemical step, a change in solute composition or equilibration with a new gas atmosphere, and spectra can be obtained over a range of time domains as far as the sub-picosecond level. We can expect to see IR spectroscopy exploited, alongside other spectroscopies, and crystallography, to elucidate reactions of a wide range of metalloprotein chemistry with relevance to cell metabolism, health and energy catalysis.

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Section: (B) Gas Exchange or Solute Exchange As A Reaction Triggermentioning

confidence: 99%

Triggered infrared spectroscopy for investigating metalloprotein chemistry

Vincent

2010

Phil. Trans. R. Soc. A.

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“…CO binding has also been investigated with electron-nuclear double resonance spectroscopy (ENDOR) [24,25]. By using stopped flow infrared spectroscopy, frequency shifts in the CO molecule upon binding could be measured [26]. CO is an inhibitor for all substrates except protons, which means that the presence of CO, all protons and electrons are used exclusively for H 2 production.…”

Section: Nitrogenase Mechanismmentioning

confidence: 99%

Catalysis by Enzymes: The Biological Ammonia Synthesis

2006

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Enzymes are nature's own catalysts and fundamental for life, as they catalyze essentially all biological processes. Compared to inorganic catalysts, however, their structure and function is immensely more complicated. Computational . modeling has played an increasing role in elucidating enzyme mechanisms, as it can provide information complementary to experimental techniques. Elucidating enzyme structure and mechanism is not only important to understand the basic functions of life, they can also help to find and develop inorganic catalysts. In this review, an overview of recent computational developments for the enzyme nitrogenase will be given. Nitrogenase catalyzes ammonia synthesis, which is also a very important reaction in inorganic catalysis, and insight on enzyme structure and function could provide understanding on how to design biomimetic catalysts for low temperature ammonia synthesis.

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“…͑2͒. 3,4 The active site of the enzyme is very well characterized, [20][21][22][23][24][25][26][27][28][29][30][31][32] but the detailed molecular mechanism is not as well established as for the metal surface process. It is generally believed that the biological process does not involve initial breaking of the N-N bond, 33 and recent DFT calculations on different Mo, Fe sulfide complexes modeling the FeMoco 34-36 support this picture.…”

Section: ͑2͒mentioning

confidence: 99%

Ammonia synthesis at low temperatures

Rod¹,

Logadóttir²,

Nørskov

2000

The Journal of Chemical Physics

227

185

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Density functional theory ͑DFT͒ calculations of reaction paths and energies for the industrial and the biological catalytic ammonia synthesis processes are compared. The industrial catalyst is modeled by a ruthenium surface, while the active part of the enzyme is modeled by a MoFe 6 S 9 complex. In contrast to the biological process, the industrial process requires high temperatures and pressures to proceed, and an explanation of this important difference is discussed. The possibility of a metal surface catalyzed process running at low temperatures and pressures is addressed, and DFT calculations have been carried out to evaluate its feasibility. The calculations suggest that it might be possible to catalytically produce ammonia from molecular nitrogen at low temperatures and pressures, in particular if energy is fed into the process electrochemically.

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Time-Resolved Binding of Carbon Monoxide to Nitrogenase Monitored by Stopped-Flow Infrared Spectroscopy

Cited by 115 publications

References 20 publications

Triggered infrared spectroscopy for investigating metalloprotein chemistry

Triggered infrared spectroscopy for investigating metalloprotein chemistry

Catalysis by Enzymes: The Biological Ammonia Synthesis

Ammonia synthesis at low temperatures

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