<link rel="stylesheet" href="styles.f3b1fba60ec7970c.css">

Theoretical Spectroscopies of Iron-Containing Enzymes and Biomimetics

Simple item page
avondale-bepress.context-key15879862
avondale-bepress.submission-pathsci_math_chapters/6
avondale.facultyScience
avondale.reporting.isPeerReviewedPeer Reviewed
avondale.reporting.versionPublished Version
dc.contributor.authorNeese, Frank
dc.contributor.authorGeng, Caiyun
dc.contributor.authorChristian, Gemma J.
dc.contributor.authorYe, Shengfa
dc.date.accessioned2023-11-01T00:29:44Z
dc.date.available2023-11-01T00:29:44Z
dc.date.issued2011-08-04
dc.date.submitted2019-11-26T20:32:30Z
dc.description.abstract<p>Spectroscopic methods play an important role in the study of iron-containing enzymes particularly for the study of reactive species, which are often difficult to characterize via crystallography. Theoretical spectroscopy, in combination with traditional quantum chemistry, is a powerful tool for the study of reactive intermediates. In this chapter the theory and applications of theoretical Mossbauer (MB), electron paramagnetic resonance (EPR), absorption spectra (ABS) and X-ray absorption spectroscopy (XAS), and nuclear resonance vibrational spectroscopy (NRVS) are described with a focus on the contribution that theoretical spectroscopy has made to the study of high-valent iron-oxo species in enzymatic and biomimetic systems.</p>
dc.identifier.citation<p>Ye, S., Christian, G. J., Geng, C., & Neese, F. (2011). Theoretical spectroscopies of iron-containing enzymes and biomimetics. In S. de Visser, & D. Kumar (Eds.), <em>Iron-containing enzymes: Versatile catalysts of hydroxylation reactions in nature</em> (pp. 119-147). Cambridge, England: Royal Society of Chemistry.</p>
dc.identifier.isbn9781849731812
dc.identifier.urihttps://research.avondale.edu.au/handle/1897/15879862
dc.language.isoen_us
dc.relation.ispartofIron-Containing Enzymes: Versatile Catalysts of Hydroxylation Reactions in Nature pp. 119-147
dc.rights<p>Copyright © 2011 Royal Society of Chemistry. All rights reserved</p> <p>Staff and Students of Avondale College may access <em>Iron-containing enzymes: Versatile catalysts of hydroxylation reactions in nature </em>from Avondale College Library (572.7517 V82)</p>
dc.subjectTheoretical Spectroscopy
dc.subjectEnzymes
dc.subjectIron
dc.subjectMossbauer
dc.subjectUV-Vis
dc.titleTheoretical Spectroscopies of Iron-Containing Enzymes and Biomimetics
dc.typeBook Chapter

Files

Collections

Science & Mathematics

Avondale University acknowledges our Sovereign God as Creator and Provider of all things. We respectfully acknowledge the Awabakal and Darramuragal people as the traditional custodians of the lands on which we live, work, study and worship across our Lake Macquarie and Sydney campuses. We pay our respects to Elders past, present and emerging, and extend that respect to all First Nations People.

Aboriginal Peoples are advised the Library Collection contains images, voices and names of deceased people in physical and online resources. The Library recognises the significance of the traditional cultural knowledges contained within its Collection. The Library acknowledge some materials contain language that may not reflect current attitudes, was published without consent or recognition, or, is offensive. These materials reflect the views of the authors and/or the period in which they were produced and do not represent the views of the Library.

Avondale University is a member of the worldwide Seventh-day Adventist system of universities and colleges.

CRICOS Provider No.: 02731D. RTO: 91191. TEQSA: PRV12015. ABN: 53 108 186 401.

© Avondale University Ltd 2026