Dr. Colin Andrew, Research Interests

l Bioinorganic Chemistry
l Metalloprotein Structure and Function
l Spectroscopic and Kinetic Studies of Metalloproteins

l Reactivity of Nitric Oxide with Heme proteins

Projects

Nitric Oxide and its Interactions with Metalloproteins

Nitric Oxide (NO) – a toxic gas found in automobile exhaust – is also an important biochemical molecule synthesized by animals, plants, and microorganisms. In 1998 the Nobel Prize for Medicine was awarded for the discovery that NO acts as a signaling molecule between cells in the cardiovascular system. Bacteria also produce NO as an intermediate during denitrification – the process by which certain organisms convert nitrate through to N₂ or N₂O. The production of NO is the first opportunity for fixed nitrogen to be lost from the soil to the atmosphere with implications ranging from fertilizer loss to atmospheric pollution. Throughout NO biochemistry, proteins with Fe or Cu-containing active sites play a central role in generating and releasing NO as well as in sensing and initiating chemistry in response to changes in NO-levels. Our research is aimed at investigating the structures and mechanisms of these metalloproteins through the use of spectroscopic, biochemical and kinetic techniques.

Selected Publications

Wilhelmina M. Huston, Colin R. Andrew, Amy E. Servid, Alison L. McKay, Andrew P. Leech, Clive S. Butler, and James W. B. Moir "Heterologous Overexpression and Purification of Cytochrome c´ from Rhodobacter capsulatus and a Mutant (K42E) in the Dimerization Region. Mutation does not alter Oligomerization but Impacts the Heme Iron Spin State and Nitric Oxide Binding Properties." Biochemistry (2006), 45, 4388-4395.

Colin R. Andrew, Lenord J. Kemper, Tammy L. Busche, Arianne M. Tiwari, Michael C. Kecskes, James M. Stafford, Lea C. Croft, Shen Lu, Pierre Moënne-Loccoz, Willa Huston, James W. B. Moir, and Robert Eady “Accessibility of the Distal Heme Face, Rather than Fe–His Bond Strength, Determines the Heme-Nitrosyl Coordination Number of  Cytochromes c´: Evidence from Spectrocopic Studies.” Biochemistry (2005), 44, 8664-8672.

Colin R. Andrew, Kenton R. Rodgers, and Robert R. Eady, “A Novel Kinetic Trap for NO Release from Cytochrome c´: A Possible Mechanism for NO Release from Activated Soluble Guanylate Cyclase.” J. Am. Chem. Soc. (2003), 125, 9548-9549.

David M. Lawson, Clare E. M. Stevenson, Colin R. Andrew, Simon J. George, and Robert R. Eady, “A two-faced molecule offers NO explanation: the proximal binding of nitric oxide to haem.” Biochem. Soc. Trans. (2003), 31, 553-557.

Colin R. Andrew, Simon J. George, David M. Lawson, and Robert R. Eady, “Six- to Five-Coordinate Heme-Nitrosyl Conversion in Cytochrome c´ and its Relevance to Guanylate Cyclase.” Biochemistry (2002), 41, 2353-2360.

Simon J. George, Colin R. Andrew, David M. Lawson, Roger N. F. Thorneley, and Robert R. Eady, “Stopped-Flow Infrared Spectroscopy Reveals a Six-Coordinate Intermediate in the Formation of the Proximally Bound Five-Coordinate NO Adduct of Cytochrome c´.” J. Am. Chem. Soc. (2001), 123, 9683-9684.

Colin R. Andrew, Edward L. Green, David M. Lawson, and Robert R. Eady, “Resonance Raman Studies of Cytochrome c´ Support the Binding of NO and CO to Opposite Sides of the Heme: Implications for Ligand Discrimination in Heme-Based Sensors.” Biochemistry (2001), 40, 4115-4122.

David M. Lawson, Clare E. M. Stevenson, Colin R. Andrew, and Robert R. Eady, “Unprecedented Proximal Binding of Nitric Oxide to Heme: Implications for Guanylate Cyclase.” EMBO J. (2000), 19, 5661-5671.

Jonathan P. Hannon, Sharon L. Davy, Geoffrey R. Moore, Robert R. Eady, and Colin R. Andrew, “Effect of Nickel(II) Substitution on the Resonance Raman and NMR Spectra of Alcaligenes xylosoxidans Azurin II: Implications for Axial-Ligand Bonding Interactions in Cupredoxin Active Sites.” J. Biol. Inorg. Chem. (1998), 3, 282-291.

Colin R. Andrew and Joann Sanders-Loehr, “Copper-Sulfur Proteins: Using Raman Spectroscopy to Predict Coordination Geometry.” Acc. Chem. Res. (1996) 29, 365-372.

Colin R. Andrew, Robert Fraczkiewicz, Roman S. Czernuszewicz, Pekka Lappalainen, Matti Saraste, and Joann Sanders-Loehr, “Identification and Description of Copper-Thiolate Vibrations in the Dinuclear Cu_A Site of Cytochrome c Oxidase.” J. Am. Chem. Soc. (1996) 118, 10436-10445.

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