Author: Jeffrey Allen GuckertPublisher:
ISBN:
Category :
Languages : en
Pages : 402
Book Description
Electronic Structure Contributions of the Blue Copper Active Site to Reduction Potentials, Geometry, and Electron Transfer Pathways
Author: Jeffrey Allen GuckertPublisher:
ISBN:
Category :
Languages : en
Pages : 402
Book Description
Spectroscopic and Theoretical Studies of Copper Containing Electron Transfer Proteins
Author: Lipika BasumallickThe Electronic Structure of the Blue Copper Proteins
Author: Kevin Wade PenfieldInvestigation of the Electronic and Geometric Structure of Copper-containing Metalloproteins Using X-ray Absorption Spectroscopy : Applications to CuA, Blue Copper, and Multicopper Oxidases
Author: Serena DeBeer GeorgePublisher:
ISBN:
Category :
Languages : en
Pages : 616
Book Description
Spectroscopic and Theoretical Studies of Perturbed Blue Copper Proteins
Author: Louis B. LaCroixStructure-function Analysis of Blue Copper Proteins
Author: Jeremy Daven KingPublisher:
ISBN:
Category : Electronic dissertations
Languages : en
Pages : 117
Book Description
Cofactors extend the chemistry of life. Redox reactions in photosynthesis, nitrogen fixation, and other metabolic pathways depend on metal cofactors. Copper is an essential element in biology, participating in redox reactions and biological catalysis. Copper proteins are classified by their copper centers as type-1, type-2, type-3, CuA, CuB, or Cuz. Type-1 proteins, such as azurin or plastocyanin, are primarily involved in electron transport. Type-1 centers are the most studied copper site at the spectroscopic and structural level. In the type-1 center, the copper cofactor is coordinated by a cysteine, two histidines, and generally a weak axial methionine. This coordination geometry gives rise to several ligand-to-metal charge-transfer transitions, producing a characteristic blue or green type-1 spectrum. In "blue" type-1 copper proteins, the cysteine-copper bond is exceptionally small (2.1 Å) and the methionine-copper bond is abnormally long (2.9 Å). In green type-1 copper proteins, the cysteine-copper bond elongates and the methionine-copper bond contracts. The redox range varies from +83 mV to over +1000 mV. Protein tuning modulates the large variations observed in the redox range and spectral properties. The mechanism of protein tuning is poorly understood. In chapter 2, I characterize a family of four blue copper proteins called auracyanins. The auracyanins, named A-D, were found to have a redox range from +83 mV to +423 mV, and range in color from blue to green. In chapter 3, I take advantage of the tuning variations within the auracyanin family to map the spectral changes to the protein-protein interaction domain. The protein-protein interaction domain has never previously been implicated in protein tuning. These results likely explain how seemingly energetically uphill electron transfer reactions commonly occur with copper proteins. In chapter 4, I perform mutagenesis on the weak axial ligand in auracyanin D. Auracyanin D is a green copper protein, and has the lowest redox potential ever measured for a copper protein. Significant work has been done on axial ligands in blue type-1 copper proteins, but never in green type-1 copper proteins. I found that substitutions to the axial ligand in green copper sites are much larger than their blue copper protein counterparts. In chapter 5, I conclude with a computational approach showing significant variation in the coordinating ligands of uncharacterized copper proteins. I believe examination of these proteins by a reverse biochemical approach will add more clarity to the role of protein tuning and expand the limits of copper tuning.
Final Report on the Joint Research Project on Structure-function Relationship in the Electron Transfer Mediating Blue Copper Proteins
Author: Israel PechtSpectroscopic and Mechanistic Studies of Copper Active Sites in Bacterial Denitrification and Cofactor Biogenesis
Author: Somdatta GhoshDissertation Abstracts International
Author: Publisher:
ISBN:
Category : Dissertations, Academic
Languages : en
Pages : 884
Book Description
Transition Metals and Sulfur – A Strong Relationship for Life
Author: Martha Sosa TorresPublisher: Walter de Gruyter GmbH & Co KG
ISBN: 3110588943
Category : Science
Languages : en
Pages : 610
Book Description
Metal Ions in Life Sciences links coordination chemistry and biochemistry in their widest sense and thus increases our understanding of the relationship between the chemistry of metals and life processes; in fact, it is an old wisdom that metals are indispensable for life. The series reflects the interdisciplinary nature of Biological Inorganic Chemistry and coordinates the efforts of scientists in numerous interconnecting research fields.