Author: Mats H. M. Olsson
Publisher:
ISBN:
Category :
Languages : en
Pages : 42
Book Description
Theoretical Studies of Blue Copper Proteins
The Electronic Structure of the Blue Copper Proteins
Spectroscopic and Theoretical Studies of Perturbed Blue Copper Proteins
Spectroscopic and Theoretical Studies of Blue Copper Proteins and Related Spectral Analogs
Spectroscopic and Theoretical Studies of Copper Containing Electron Transfer Proteins
Copper Proteins and Copper Enzymes
Author: Rene Lontie
Publisher: CRC Press
ISBN: 1351079352
Category : Medical
Languages : en
Pages : 233
Book Description
These volumes of Copper Proteins and Copper Enzymes are intended to describe the contemporary spectroscopy and other biophysical chemistry now being applied to copper proteins in order to determine the structures of their active sites. Several chapters of the treatise describe the functional understanding which is emerging from the new work. The authors are all major contributors to research progress on copper proteins and the volumes will be found to be definitive and authoritative.
Publisher: CRC Press
ISBN: 1351079352
Category : Medical
Languages : en
Pages : 233
Book Description
These volumes of Copper Proteins and Copper Enzymes are intended to describe the contemporary spectroscopy and other biophysical chemistry now being applied to copper proteins in order to determine the structures of their active sites. Several chapters of the treatise describe the functional understanding which is emerging from the new work. The authors are all major contributors to research progress on copper proteins and the volumes will be found to be definitive and authoritative.
X-ray Absorption Spectroscopic and Theoretical Studies on Copper Containing Proteins
Structure-function Analysis of Blue Copper Proteins
Author: Jeremy Daven King
Publisher:
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.
Publisher:
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.
Metal Sites in Proteins and Models
Author: H.A.O. Hill
Publisher: Springer Science & Business Media
ISBN: 9783540655534
Category : Science
Languages : en
Pages : 222
Book Description
Biological chemistry is a major frontier of inorganic chemistry. Three special volumes devoted to Metal Sites in Proteins and Models address the questions: how unusual ("entatic") are metal sites in metalloproteins and metalloenzymes compared to those in small coordination complexes? and if they are special, how do polypeptide chains and co-factors control this? The chapters deal with iron, with metal centres acting as Lewis acids, metals in phosphate enzymes, with vanadium, and with the wide variety of transition metal ions which act as redox centres. They illustrate in particular how the combined armoury of genetics and structure determination at the molecular level are providing unprecedented new tools for molecular engineering.
Publisher: Springer Science & Business Media
ISBN: 9783540655534
Category : Science
Languages : en
Pages : 222
Book Description
Biological chemistry is a major frontier of inorganic chemistry. Three special volumes devoted to Metal Sites in Proteins and Models address the questions: how unusual ("entatic") are metal sites in metalloproteins and metalloenzymes compared to those in small coordination complexes? and if they are special, how do polypeptide chains and co-factors control this? The chapters deal with iron, with metal centres acting as Lewis acids, metals in phosphate enzymes, with vanadium, and with the wide variety of transition metal ions which act as redox centres. They illustrate in particular how the combined armoury of genetics and structure determination at the molecular level are providing unprecedented new tools for molecular engineering.
Theoretical Biochemistry
Author: Leif A. Eriksson
Publisher: Elsevier
ISBN: 0080542700
Category : Science
Languages : en
Pages : 719
Book Description
Theoretical chemistry has been an area of tremendous expansion and development over the past decade; from an approach where we were able to treat only a few atoms quantum mechanically or make fairly crude molecular dynamics simulations, into a discipline with an accuracy and predictive power that has rendered it an essential complementary tool to experiment in basically all areas of science. This volume gives a flavour of the types of problems in biochemistry that theoretical calculations can solve at present, and illustrates the tremendous predictive power these approaches possess.A wide range of computational approaches, from classical MD and Monte Carlo methods, via semi-empirical and DFT approaches on isolated model systems, to Car-Parinello QM-MD and novel hybrid QM/MM studies are covered. The systems investigated also cover a broad range; from membrane-bound proteins to various types of enzymatic reactions as well as inhibitor studies, cofactor properties, solvent effects, transcription and radiation damage to DNA.
Publisher: Elsevier
ISBN: 0080542700
Category : Science
Languages : en
Pages : 719
Book Description
Theoretical chemistry has been an area of tremendous expansion and development over the past decade; from an approach where we were able to treat only a few atoms quantum mechanically or make fairly crude molecular dynamics simulations, into a discipline with an accuracy and predictive power that has rendered it an essential complementary tool to experiment in basically all areas of science. This volume gives a flavour of the types of problems in biochemistry that theoretical calculations can solve at present, and illustrates the tremendous predictive power these approaches possess.A wide range of computational approaches, from classical MD and Monte Carlo methods, via semi-empirical and DFT approaches on isolated model systems, to Car-Parinello QM-MD and novel hybrid QM/MM studies are covered. The systems investigated also cover a broad range; from membrane-bound proteins to various types of enzymatic reactions as well as inhibitor studies, cofactor properties, solvent effects, transcription and radiation damage to DNA.