The Experts below are selected from a list of 198 Experts worldwide ranked by ideXlab platform
Jeanlouis Martin - One of the best experts on this subject based on the ideXlab platform.
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low frequency vibrational modes in proteins changes induced by point mutations in the protein Cofactor Matrix of bacterial reaction centers
Proceedings of the National Academy of Sciences of the United States of America, 1998Co-Authors: Christian Rischel, Diane Spiedel, Justin P Ridge, M R Jones, Jacques Breton, Jeanchristophe Lambry, Jeanlouis MartinAbstract:As a step toward understanding their functional role, the low frequency vibrational motions (<300 cm−1) that are coupled to optical excitation of the primary donor bacteriochlorophyll Cofactors in the reaction center from Rhodobacter sphaeroides were investigated. The pattern of hydrogen-bonding interaction between these bacteriochlorophylls and the surrounding protein was altered in several ways by mutation of single amino acids. The spectrum of low frequency vibrational modes identified by femtosecond coherence spectroscopy varied strongly between the different reaction center complexes, including between different mutants where the pattern of hydrogen bonds was the same. It is argued that these variations are primarily due to changes in the nature of the individual modes, rather than to changes in the charge distribution in the electronic states involved in the optical excitation. Pronounced effects of point mutations on the low frequency vibrational modes active in a protein-Cofactor system have not been reported previously. The changes in frequency observed indicate a strong involvement of the protein in these nuclear motions and demonstrate that the protein Matrix can increase or decrease the fluctuations of the Cofactor along specific directions.
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Low frequency vibrational modes in proteins: Changes induced by point-mutations in the protein-Cofactor Matrix of bacterial reaction centers
Proceedings of the National Academy of Sciences of the United States of America, 1998Co-Authors: Christian Rischel, Diane Spiedel, Justin P Ridge, M R Jones, Jacques Breton, Jeanchristophe Lambry, Jeanlouis MartinAbstract:As a step toward understanding their functional role, the low frequency vibrational motions (
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Changes in Low-Frequency Vibrational Modes Induced by Point-Mutations in the Protein-Cofactor Matrix of Bacterial Reaction Centers
Photosynthesis: Mechanisms and Effects, 1998Co-Authors: Christian Rischel, Diane Spiedel, Justin P Ridge, M R Jones, Jacques Breton, Jeanchristophe Lambry, Jeanlouis MartinAbstract:The formation of the excited state P* of the primary donor of bacterial RCs sets in motion low-frequency (mostly
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changes in low frequency vibrational modes induced by point mutations in the protein Cofactor Matrix of bacterial reaction centers
XIth International Congress on Photosynthesis - Mechanisms and Effects, 1998Co-Authors: Christian Rischel, Diane Spiedel, Justin P Ridge, M R Jones, Jacques Breton, Jeanchristophe Lambry, Jeanlouis MartinAbstract:The formation of the excited state P* of the primary donor of bacterial RCs sets in motion low-frequency (mostly <250 cm-1) vibrational motions [1]. These motions are coherent and persist on the time scale of primary electron transfer. The molecular ‘identity’ of these motions is essentially unknown. Their low frequency suggests that they are delocalized over the protein environment to a certain extent. In the present work, we have examined the effects of modification of the bonding between the Cofactors and protein, by studying mutants designed to add or remove hydrogen bonds between the protein and the Bchls of P [2]. In WT, one hydrogen bond between the 2-acetyl carbonyl group of PL and His L168 is present. Using low-temperature femtosecond spectroscopy, we compared the frequency spectrum of membrane-bound RCs from WT with mutants in which this hydrogen bond had been deleted by replacement of HL168 by F, L or D, and where a second hydrogen bond has been introduced at the 2-acetyl carbonyl group of PM (FM197H) and at the 9-keto carbonyl group of Pm (LL131H).
Christian Rischel - One of the best experts on this subject based on the ideXlab platform.
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low frequency vibrational modes in proteins changes induced by point mutations in the protein Cofactor Matrix of bacterial reaction centers
Proceedings of the National Academy of Sciences of the United States of America, 1998Co-Authors: Christian Rischel, Diane Spiedel, Justin P Ridge, M R Jones, Jacques Breton, Jeanchristophe Lambry, Jeanlouis MartinAbstract:As a step toward understanding their functional role, the low frequency vibrational motions (<300 cm−1) that are coupled to optical excitation of the primary donor bacteriochlorophyll Cofactors in the reaction center from Rhodobacter sphaeroides were investigated. The pattern of hydrogen-bonding interaction between these bacteriochlorophylls and the surrounding protein was altered in several ways by mutation of single amino acids. The spectrum of low frequency vibrational modes identified by femtosecond coherence spectroscopy varied strongly between the different reaction center complexes, including between different mutants where the pattern of hydrogen bonds was the same. It is argued that these variations are primarily due to changes in the nature of the individual modes, rather than to changes in the charge distribution in the electronic states involved in the optical excitation. Pronounced effects of point mutations on the low frequency vibrational modes active in a protein-Cofactor system have not been reported previously. The changes in frequency observed indicate a strong involvement of the protein in these nuclear motions and demonstrate that the protein Matrix can increase or decrease the fluctuations of the Cofactor along specific directions.
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Low frequency vibrational modes in proteins: Changes induced by point-mutations in the protein-Cofactor Matrix of bacterial reaction centers
Proceedings of the National Academy of Sciences of the United States of America, 1998Co-Authors: Christian Rischel, Diane Spiedel, Justin P Ridge, M R Jones, Jacques Breton, Jeanchristophe Lambry, Jeanlouis MartinAbstract:As a step toward understanding their functional role, the low frequency vibrational motions (
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Changes in Low-Frequency Vibrational Modes Induced by Point-Mutations in the Protein-Cofactor Matrix of Bacterial Reaction Centers
Photosynthesis: Mechanisms and Effects, 1998Co-Authors: Christian Rischel, Diane Spiedel, Justin P Ridge, M R Jones, Jacques Breton, Jeanchristophe Lambry, Jeanlouis MartinAbstract:The formation of the excited state P* of the primary donor of bacterial RCs sets in motion low-frequency (mostly
-
changes in low frequency vibrational modes induced by point mutations in the protein Cofactor Matrix of bacterial reaction centers
XIth International Congress on Photosynthesis - Mechanisms and Effects, 1998Co-Authors: Christian Rischel, Diane Spiedel, Justin P Ridge, M R Jones, Jacques Breton, Jeanchristophe Lambry, Jeanlouis MartinAbstract:The formation of the excited state P* of the primary donor of bacterial RCs sets in motion low-frequency (mostly <250 cm-1) vibrational motions [1]. These motions are coherent and persist on the time scale of primary electron transfer. The molecular ‘identity’ of these motions is essentially unknown. Their low frequency suggests that they are delocalized over the protein environment to a certain extent. In the present work, we have examined the effects of modification of the bonding between the Cofactors and protein, by studying mutants designed to add or remove hydrogen bonds between the protein and the Bchls of P [2]. In WT, one hydrogen bond between the 2-acetyl carbonyl group of PL and His L168 is present. Using low-temperature femtosecond spectroscopy, we compared the frequency spectrum of membrane-bound RCs from WT with mutants in which this hydrogen bond had been deleted by replacement of HL168 by F, L or D, and where a second hydrogen bond has been introduced at the 2-acetyl carbonyl group of PM (FM197H) and at the 9-keto carbonyl group of Pm (LL131H).
Jeanchristophe Lambry - One of the best experts on this subject based on the ideXlab platform.
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low frequency vibrational modes in proteins changes induced by point mutations in the protein Cofactor Matrix of bacterial reaction centers
Proceedings of the National Academy of Sciences of the United States of America, 1998Co-Authors: Christian Rischel, Diane Spiedel, Justin P Ridge, M R Jones, Jacques Breton, Jeanchristophe Lambry, Jeanlouis MartinAbstract:As a step toward understanding their functional role, the low frequency vibrational motions (<300 cm−1) that are coupled to optical excitation of the primary donor bacteriochlorophyll Cofactors in the reaction center from Rhodobacter sphaeroides were investigated. The pattern of hydrogen-bonding interaction between these bacteriochlorophylls and the surrounding protein was altered in several ways by mutation of single amino acids. The spectrum of low frequency vibrational modes identified by femtosecond coherence spectroscopy varied strongly between the different reaction center complexes, including between different mutants where the pattern of hydrogen bonds was the same. It is argued that these variations are primarily due to changes in the nature of the individual modes, rather than to changes in the charge distribution in the electronic states involved in the optical excitation. Pronounced effects of point mutations on the low frequency vibrational modes active in a protein-Cofactor system have not been reported previously. The changes in frequency observed indicate a strong involvement of the protein in these nuclear motions and demonstrate that the protein Matrix can increase or decrease the fluctuations of the Cofactor along specific directions.
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Low frequency vibrational modes in proteins: Changes induced by point-mutations in the protein-Cofactor Matrix of bacterial reaction centers
Proceedings of the National Academy of Sciences of the United States of America, 1998Co-Authors: Christian Rischel, Diane Spiedel, Justin P Ridge, M R Jones, Jacques Breton, Jeanchristophe Lambry, Jeanlouis MartinAbstract:As a step toward understanding their functional role, the low frequency vibrational motions (
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Changes in Low-Frequency Vibrational Modes Induced by Point-Mutations in the Protein-Cofactor Matrix of Bacterial Reaction Centers
Photosynthesis: Mechanisms and Effects, 1998Co-Authors: Christian Rischel, Diane Spiedel, Justin P Ridge, M R Jones, Jacques Breton, Jeanchristophe Lambry, Jeanlouis MartinAbstract:The formation of the excited state P* of the primary donor of bacterial RCs sets in motion low-frequency (mostly
-
changes in low frequency vibrational modes induced by point mutations in the protein Cofactor Matrix of bacterial reaction centers
XIth International Congress on Photosynthesis - Mechanisms and Effects, 1998Co-Authors: Christian Rischel, Diane Spiedel, Justin P Ridge, M R Jones, Jacques Breton, Jeanchristophe Lambry, Jeanlouis MartinAbstract:The formation of the excited state P* of the primary donor of bacterial RCs sets in motion low-frequency (mostly <250 cm-1) vibrational motions [1]. These motions are coherent and persist on the time scale of primary electron transfer. The molecular ‘identity’ of these motions is essentially unknown. Their low frequency suggests that they are delocalized over the protein environment to a certain extent. In the present work, we have examined the effects of modification of the bonding between the Cofactors and protein, by studying mutants designed to add or remove hydrogen bonds between the protein and the Bchls of P [2]. In WT, one hydrogen bond between the 2-acetyl carbonyl group of PL and His L168 is present. Using low-temperature femtosecond spectroscopy, we compared the frequency spectrum of membrane-bound RCs from WT with mutants in which this hydrogen bond had been deleted by replacement of HL168 by F, L or D, and where a second hydrogen bond has been introduced at the 2-acetyl carbonyl group of PM (FM197H) and at the 9-keto carbonyl group of Pm (LL131H).
Jacques Breton - One of the best experts on this subject based on the ideXlab platform.
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low frequency vibrational modes in proteins changes induced by point mutations in the protein Cofactor Matrix of bacterial reaction centers
Proceedings of the National Academy of Sciences of the United States of America, 1998Co-Authors: Christian Rischel, Diane Spiedel, Justin P Ridge, M R Jones, Jacques Breton, Jeanchristophe Lambry, Jeanlouis MartinAbstract:As a step toward understanding their functional role, the low frequency vibrational motions (<300 cm−1) that are coupled to optical excitation of the primary donor bacteriochlorophyll Cofactors in the reaction center from Rhodobacter sphaeroides were investigated. The pattern of hydrogen-bonding interaction between these bacteriochlorophylls and the surrounding protein was altered in several ways by mutation of single amino acids. The spectrum of low frequency vibrational modes identified by femtosecond coherence spectroscopy varied strongly between the different reaction center complexes, including between different mutants where the pattern of hydrogen bonds was the same. It is argued that these variations are primarily due to changes in the nature of the individual modes, rather than to changes in the charge distribution in the electronic states involved in the optical excitation. Pronounced effects of point mutations on the low frequency vibrational modes active in a protein-Cofactor system have not been reported previously. The changes in frequency observed indicate a strong involvement of the protein in these nuclear motions and demonstrate that the protein Matrix can increase or decrease the fluctuations of the Cofactor along specific directions.
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Low frequency vibrational modes in proteins: Changes induced by point-mutations in the protein-Cofactor Matrix of bacterial reaction centers
Proceedings of the National Academy of Sciences of the United States of America, 1998Co-Authors: Christian Rischel, Diane Spiedel, Justin P Ridge, M R Jones, Jacques Breton, Jeanchristophe Lambry, Jeanlouis MartinAbstract:As a step toward understanding their functional role, the low frequency vibrational motions (
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Changes in Low-Frequency Vibrational Modes Induced by Point-Mutations in the Protein-Cofactor Matrix of Bacterial Reaction Centers
Photosynthesis: Mechanisms and Effects, 1998Co-Authors: Christian Rischel, Diane Spiedel, Justin P Ridge, M R Jones, Jacques Breton, Jeanchristophe Lambry, Jeanlouis MartinAbstract:The formation of the excited state P* of the primary donor of bacterial RCs sets in motion low-frequency (mostly
-
changes in low frequency vibrational modes induced by point mutations in the protein Cofactor Matrix of bacterial reaction centers
XIth International Congress on Photosynthesis - Mechanisms and Effects, 1998Co-Authors: Christian Rischel, Diane Spiedel, Justin P Ridge, M R Jones, Jacques Breton, Jeanchristophe Lambry, Jeanlouis MartinAbstract:The formation of the excited state P* of the primary donor of bacterial RCs sets in motion low-frequency (mostly <250 cm-1) vibrational motions [1]. These motions are coherent and persist on the time scale of primary electron transfer. The molecular ‘identity’ of these motions is essentially unknown. Their low frequency suggests that they are delocalized over the protein environment to a certain extent. In the present work, we have examined the effects of modification of the bonding between the Cofactors and protein, by studying mutants designed to add or remove hydrogen bonds between the protein and the Bchls of P [2]. In WT, one hydrogen bond between the 2-acetyl carbonyl group of PL and His L168 is present. Using low-temperature femtosecond spectroscopy, we compared the frequency spectrum of membrane-bound RCs from WT with mutants in which this hydrogen bond had been deleted by replacement of HL168 by F, L or D, and where a second hydrogen bond has been introduced at the 2-acetyl carbonyl group of PM (FM197H) and at the 9-keto carbonyl group of Pm (LL131H).
M R Jones - One of the best experts on this subject based on the ideXlab platform.
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low frequency vibrational modes in proteins changes induced by point mutations in the protein Cofactor Matrix of bacterial reaction centers
Proceedings of the National Academy of Sciences of the United States of America, 1998Co-Authors: Christian Rischel, Diane Spiedel, Justin P Ridge, M R Jones, Jacques Breton, Jeanchristophe Lambry, Jeanlouis MartinAbstract:As a step toward understanding their functional role, the low frequency vibrational motions (<300 cm−1) that are coupled to optical excitation of the primary donor bacteriochlorophyll Cofactors in the reaction center from Rhodobacter sphaeroides were investigated. The pattern of hydrogen-bonding interaction between these bacteriochlorophylls and the surrounding protein was altered in several ways by mutation of single amino acids. The spectrum of low frequency vibrational modes identified by femtosecond coherence spectroscopy varied strongly between the different reaction center complexes, including between different mutants where the pattern of hydrogen bonds was the same. It is argued that these variations are primarily due to changes in the nature of the individual modes, rather than to changes in the charge distribution in the electronic states involved in the optical excitation. Pronounced effects of point mutations on the low frequency vibrational modes active in a protein-Cofactor system have not been reported previously. The changes in frequency observed indicate a strong involvement of the protein in these nuclear motions and demonstrate that the protein Matrix can increase or decrease the fluctuations of the Cofactor along specific directions.
-
Low frequency vibrational modes in proteins: Changes induced by point-mutations in the protein-Cofactor Matrix of bacterial reaction centers
Proceedings of the National Academy of Sciences of the United States of America, 1998Co-Authors: Christian Rischel, Diane Spiedel, Justin P Ridge, M R Jones, Jacques Breton, Jeanchristophe Lambry, Jeanlouis MartinAbstract:As a step toward understanding their functional role, the low frequency vibrational motions (
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Changes in Low-Frequency Vibrational Modes Induced by Point-Mutations in the Protein-Cofactor Matrix of Bacterial Reaction Centers
Photosynthesis: Mechanisms and Effects, 1998Co-Authors: Christian Rischel, Diane Spiedel, Justin P Ridge, M R Jones, Jacques Breton, Jeanchristophe Lambry, Jeanlouis MartinAbstract:The formation of the excited state P* of the primary donor of bacterial RCs sets in motion low-frequency (mostly
-
changes in low frequency vibrational modes induced by point mutations in the protein Cofactor Matrix of bacterial reaction centers
XIth International Congress on Photosynthesis - Mechanisms and Effects, 1998Co-Authors: Christian Rischel, Diane Spiedel, Justin P Ridge, M R Jones, Jacques Breton, Jeanchristophe Lambry, Jeanlouis MartinAbstract:The formation of the excited state P* of the primary donor of bacterial RCs sets in motion low-frequency (mostly <250 cm-1) vibrational motions [1]. These motions are coherent and persist on the time scale of primary electron transfer. The molecular ‘identity’ of these motions is essentially unknown. Their low frequency suggests that they are delocalized over the protein environment to a certain extent. In the present work, we have examined the effects of modification of the bonding between the Cofactors and protein, by studying mutants designed to add or remove hydrogen bonds between the protein and the Bchls of P [2]. In WT, one hydrogen bond between the 2-acetyl carbonyl group of PL and His L168 is present. Using low-temperature femtosecond spectroscopy, we compared the frequency spectrum of membrane-bound RCs from WT with mutants in which this hydrogen bond had been deleted by replacement of HL168 by F, L or D, and where a second hydrogen bond has been introduced at the 2-acetyl carbonyl group of PM (FM197H) and at the 9-keto carbonyl group of Pm (LL131H).