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Dr. A. Galkin

Dr. Alexander Galkin
Dr. Alexander Galkin
Lecturer in Biochemistry
PhD Biochemistry, Moscow State University, 2001.

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Contact Information
Tel:  +44 (0)28 9097 2166 (Direct line)
Fax:  +44 (0)28 9097 5877
Email:  a.galkin@qub.ac.uk
Address: Medical Biology Centre, room 01.442
            School of Biological Sciences
            Queen's University Belfast
            Belfast, BT9 7BL, United Kingdom

Funded by:       

 

POSITION AVAILABLE


 

Research Interests: Mitochondria and Ischaemia/Reperfusion 

My main interests are bioenergetics and mitochondrial biochemistry, in particular the behaviour of mitochondrial Complex I in pathological conditions such as hypoxia or ischaemia/reperfusion.  The enzyme is located at an entry point of the electron transport chain and catalyses electron transfer from NADH to ubiquinone (Coenzyme Q).  This large multisubunit membrane enzyme occupies a key position in cell metabolism and energy production and is responsible for oxidation of matrix NADH. Dysfunction of Complex I is involved in pathological conditions such as Parkinson's disease, various encephalomyopathies and the process of aging.  Mitochondrial complex I is a major target during cardiac ischemia/reperfusion. Despite the importance of Complex I for cellular metabolism, little is known about its regulation in vivo.  The mammalian enzyme exists in two conformationally distinct, interconvertible forms - active (A) and dormant, de-active (D), but the physiological role of A/D transition is not understood.  We aim to gain a clearer understanding of the role of A/D transition, the way in which Complex I regulates the response of cells to hypoxia, and how this regulation is influenced by natural effectors including nitric oxide and ROS. Read more...


Subunits involved into ischemic active/dormant transition of mitochondrial complex I (based on PDB ID: 4WZ7). The protein is shown in grey and subunits involved into transition shown in color using a cartoon representation (ND3 red, ND1 pink, PSST blue, 49 kDa beige, 39 kDa green). Iron–sulfur clusters are represented as yellow spheres. Schematic conformational change of partially resolved hydrophilic loop of ND3 THM 1-2ND3 in the A and in the D-form is shown at the end of the clip.