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Instruments / Technical Area	Publication Details	Published
	Measuring protein dynamics with ultrafast two-dimensional infrared spectroscopy Katrin Adamczyk , Marco Candelaresi , Kirsty Robb , Andrea Gumiero , Martin A. Walsh , Anthony W. Parker , Paul A. Hoskisson , Nicholas P. Tucker , Neil T. Hunt Measurement Science And Technology 23 (6) DOI: 10.1088/0957-0233/23/6/062001 Show Abstract ▼ Abstract: Recent advances in the methodology and application of ultrafast two-dimensional infrared (2D-IR) spectroscopy to biomolecular systems are reviewed. A description of the 2D-IR technique and the molecular contributions to the observed spectra are presented followed by a discussion of recent literature relating to the use of 2D-IR and associated approaches for measuring protein dynamics. In particular, these include the use of diatomic ligand groups for measuring haem protein dynamics, isotopic labelling strategies and the use of vibrational probe groups. The final section reports on the current state of the art regarding the use of 2D-IR methods to provide insights into biological reaction mechanisms.	Jun 2012
I03-Macromolecular Crystallography I04-Macromolecular Crystallography	An analysis of substrate binding interactions in the heme peroxidase enzymes Andrea Gumiero , Emma J. Murphy , Clive L. Metcalfe , Peter C. E. Moody , Emma L. Raven Archives Of Biochemistry And Biophysics 500 (1), 13-20 DOI: 10.1016/j.abb.2010.02.015 PMID: 20206594 Diamond Proposal Number(s): [310] Show Abstract ▼ Abstract: The interactions of heme peroxidase enzymes with their substrates have been studied for many years, but only in the last decade or so has structural information begun to appear. This review looks at crystal structures for a number of heme peroxidases in complex with a number of (mainly organic) substrates. It examines the nature and location of the binding interaction, and explores functional similarities and differences across the family.	Mar 2010
I04-Macromolecular Crystallography	Nature of the ferryl heme in compounds I and II Andrea Gumiero , Clive L. Metcalfe , Emma Raven , Peter C. E. Moody , Arwen Pearson Journal Of Biological Chemistry 286, 1260-1268. DOI: 10.1074/jbc.M110.183483 PMID: 21062738 Diamond Proposal Number(s): [6388] Open Access Show Abstract ▼ Abstract: Heme enzymes are ubiquitous in biology and catalyze a vast array of biological redox processes. The formation of high valent ferryl intermediates of the heme iron (known as Compounds I and Compound II) is implicated for a number of catalytic heme enzymes, but these species are formed only transiently and thus have proved somewhat elusive. In consequence, there has been conflicting evidence as to the nature of these ferryl intermediates in a number of different heme enzymes, in particular the precise nature of the bond between the heme iron and the bound oxygen atom. In this work, we present high resolution crystal structures of both Compound I and Compound II intermediates in two different heme peroxidase enzymes, cytochrome c peroxidase and ascorbate peroxidase, allowing direct and accurate comparison of the bonding interactions in the different intermediates. A consistent picture emerges across all structures, showing lengthening of the ferryl oxygen bond (and presumed protonation) on reduction of Compound I to Compound II. These data clarify long standing inconsistencies on the nature of the ferryl heme species in these intermediates.	Jan 2011

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