Dr
Allen Orville
(Brookhaven National Laboratory)
05/07/2012, 13:00
Invited oral contribution
We are creating a multidisciplinary, high throughput pipeline for the structural and biophysical analysis of macromolecules involved in bacterial N2-fixation in plants. Sinorhizobium meliloti 1021 and WSM419 are free-living or N2-fixing microbes. But, they only fix N2 under symbiotic, microaerobic conditions within root nodules of legumes such as alfalfa and its diploid model, Medicago...
Dr
Hough Michael
(University of Essex)
05/07/2012, 13:30
Biological / Pharmaceutical Research
Oral contribution
Single crystal spectroscopic analysis may be used to gain a complete and accurate identification of the redox and ligation states of metal (redox) centres in protein crystals [1,2]. Combining this approach with controlled X-ray radiolysis can allow the generation and characterisation of functional species and intermediates [3].
Cytochrome c’ (CYTcp) is a haem protein with the remarkable...
Dr
Markus Knipp
(Max-Planck-Institut für Bioanorganische Chemie)
05/07/2012, 13:50
Biological / Pharmaceutical Research
Oral contribution
Nitrophorin 4 (NP4) is a ferriheme protein that is found in the saliva of the blood-sucking insect Rhodnius prolixus. The purpose of the protein is to transport NO from the saliva of the insect into the tissue of a victim, for which purpose the heme iron is maintained in the Fe(III) state. A novel protein mutant NP4(L130R) was generated to explore the recently reported nitrite...
Mr
Christian Martinoli
(University of Pavia)
05/07/2012, 14:10
Biological / Pharmaceutical Research
Oral contribution
Baeyer-Villiger monooxygenases (BVMOs) are promising targets for biocatalytic applications in synthetic and pharmaceutical chemistry. These flavoenzymes mainly convert ketones into their corresponding esters using NAD(P)H as electron donor by catalyzing the insertion of a single oxygen atom nearby the carbonyl group. Fundamental property of BVMOs is their ability to stabilize the...
Dr
Hans-Petter Hersleth
(Department of Molecular Biosciences, University of Oslo, P.O.Box 1041 Blindern, 0316 Oslo, Norway)
05/07/2012, 14:30
Biological / Pharmaceutical Research
Oral contribution
To be able to correctly interpret the crystal structure of redox- and metalloproteins caution must be employed. The influence of X-ray radiation damage to protein crystals is well known to occur even at cryogenic temperatures, and redox active sites like metal sites seem especially vulnerable for radiation-induced reduction [1,2,3]. We have used in situ (online) UV-vis and Raman spectroscopy...
