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Alexander Galkin


Tel:  +44 (0)28 9097 2166 (Direct line)
         +1 3472556550          (Mob)
Fax:  +44 (0)28 9097 5877  
Email:  a.galkin@qub.ac.uk    OR                           uncoupler@gmail.com


Address: 

Medical Biology Centre, room 01.442
School of Biological Sciences
Queen's University Belfast
Belfast, BT9 7BL, United Kingdom

OR
  
Feil Family Brain and Mind Research Institute, Weill Cornell Medical College,
407 East 61st Street; 5th floor,
New York, NY 10065
  

The main focus of our research is mitochondrial Complex I and conformational changes of the enzyme  in hypoxia.

Subunits involved into ischemic active/deactive (A/D) transition of mitochondrial complex I (based on PDB ID: 4WZ7). The protein is shown in grey and subunits involved into transition shown in colour 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 THM1-2ND3 in the A and in the D-form is shown at the end of the clip.

CONTACT

Alexander Galkin, Cornell Medical College, Queens University
Research Interests: 

  My maiin interests are bioenergetics and mitochondrial biochemistry, in particular the behaviour of mitochondrial Complex I in pathological conditions such as hypoxia or ischemia/reperfusion.  The enzyme is located at the 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 brain and 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)