Výsledky vyhledávání

Akademický článek

Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.

Periodical

Fluorinated TRISPHAT Anions: Spectroscopic Probes for Detailed Asymmetric Ion Pairing StudiesWe thank Prof. Ian Dance for helpful discussions and preliminary calculations and Prof. Alceo Macchioni for his expert advice on HOESY NMR experiments. We are grateful for financial support of this work by the Swiss National Science Foundation, the Federal Office for Education and Science, and the Sandoz Family Foundation (R.F., J.L.).

Autor: Frantz, Richard, Pinto, André, Constant, Samuel, Bernardinelli, Gérald, Lacour, Jérôme

Publikováno v: Angewandte Chemie. International Edition; August 2005, Vol. 44 Issue: 32 p5060-5064, 5p

Zobrazit plný text záznamu

The binding of reducible N2 in the reaction domain of nitrogenase

Autor: Ian Dance

Publikováno v: Dalton Transactions. 52:2013-2026

Promotional N2 (for the HD reaction of nitrogenase) binding at the exo-Fe2 position of FeMo-co allows reducible N2 (forming NH3) to diffuse in and bind exergonically at the endo coordination position of Fe2 or Fe6 in the central reaction domain.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::8301c9ad10f66b77350041be69ee3dca
https://doi.org/10.1039/d2dt03599e

Zobrazit plný text záznamu

Periodical

Precious metal: Ian Dance performs some fancy footwork with his new Daf CF drawbar, CMG specialising in shifting valuable classic cars. Being careful is the name of this game...

Autor: Dunn, Pip

Publikováno v: Truck & Driver. Jul2017, p74-79. 6p.

Zobrazit plný text záznamu

Understanding the tethered unhooking and rehooking of S2B in the reaction domain of FeMo-co, the active site of nitrogenase

Autor: Ian Dance

Publikováno v: Dalton Transactions. 51:15538-15554

Energetically accessible reversible unhooking of S2B or S2BH from Fe2, as an intrinsic property of FeMo-co, needs to be considered in the formulation of mechanisms for the reactions of nitrogenase.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a08bcc1b7749dad6ea66a09a0b8b76d8
https://doi.org/10.1039/d2dt02571j

Zobrazit plný text záznamu

Calculating the chemical mechanism of nitrogenase: new working hypotheses

Autor: Ian Dance

Publikováno v: Dalton transactions (Cambridge, England : 2003). 51(33)

Additional working hypotheses for the mechanism of the enzyme nitrogenase: the active site uses several binding sites with different mechanistic roles.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7930ae6e8e973de324d08df4a4e28c7f
https://pubmed.ncbi.nlm.nih.gov/35946501

Zobrazit plný text záznamu

The HD Reaction of Nitrogenase: a Detailed Mechanism

Autor: Ian Dance

Publikováno v: Chemistry (Weinheim an der Bergstrasse, Germany).

Nitrogenase is the enzyme that converts N

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::34eb8eb875a6e140ea170571dbe97228
https://pubmed.ncbi.nlm.nih.gov/36274057

Zobrazit plný text záznamu

Akademický článek

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

Autor: Ian Dance

Publikováno v: Inorganics, Vol 7, Iss 1, p 8 (2019)

The enzyme nitrogenase naturally hydrogenates N2 to NH3, achieved through the accumulation of H atoms on FeMo-co, the Fe7MoS9C(homocitrate) cluster that is the catalytically active site. Four intermediates, E1H1, E2H2, E3H3, and E4H4, carry these hyd

Externí odkaz: https://doaj.org/article/85dfd74a4db546d99346314452c00704

Zobrazit plný text záznamu

Plný text ve formátu HTML

Vyhledávací nástroje:

Upřesnit hledání