LIVIVO - Search results -

Search results

Result 1 - 10 of total 126

Search options

Article ; Online: Catalysis by Nature's photoenzymes.

Taylor, Aoife / Heyes, Derren J / Scrutton, Nigel S

2022 Volume 77, Page(s) 102491

Abstract: Photoenzymes use light to initiate biochemical reactions. Although rarely found in nature, their study has advanced understanding of how light energy can be harnessed to facilitate enzyme catalysis, which is also of importance to the design and ... ...

Abstract	Photoenzymes use light to initiate biochemical reactions. Although rarely found in nature, their study has advanced understanding of how light energy can be harnessed to facilitate enzyme catalysis, which is also of importance to the design and engineering of man-made photocatalysts. Natural photoenzymes can be assigned to one of two families, based broadly on the nature of the light-sensing chromophores used, those being chlorophyll-like tetrapyrroles or flavins. In all cases, light absorption leads to excited state electron transfer, which in turn initiates photocatalysis. Reviewed here are recent findings relating to the structures and mechanisms of known photoenzymes. We highlight recent advances that have deepened understanding of mechanisms in biological photocatalysis.
Language	English
Publishing date	2022-10-30
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1068353-7
ISSN	1879-033X ; 0959-440X
ISSN (online)	1879-033X
ISSN	0959-440X
DOI	10.1016/j.sbi.2022.102491
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 3206: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Details ▾
- See ZB MED holdings
- Order with fees

Article: A guide to time‐resolved structural analysis of light‐activated proteins

Poddar, Harshwardhan / Heyes, Derren J. / Schirò, Giorgio / Weik, Martin / Leys, David / Scrutton, Nigel S.

FEBS journal. 2022 Feb., v. 289, no. 3

2022

Abstract: Dynamical changes in protein structures are essential for protein function and occur over femtoseconds to seconds timescales. X‐ray free electron lasers have facilitated investigations of structural dynamics in proteins with unprecedented temporal and ... ...

Abstract	Dynamical changes in protein structures are essential for protein function and occur over femtoseconds to seconds timescales. X‐ray free electron lasers have facilitated investigations of structural dynamics in proteins with unprecedented temporal and spatial resolution. Light‐activated proteins are attractive targets for time‐resolved structural studies, as the reaction chemistry and associated protein structural changes can be triggered by short laser pulses. Proteins with different light‐absorbing centres have evolved to detect light and harness photon energy to bring about downstream chemical and biological output responses. Following light absorption, rapid chemical/small‐scale structural changes are typically localised around the chromophore. These localised changes are followed by larger structural changes propagated throughout the photoreceptor/photocatalyst that enables the desired chemical and/or biological output response. Time‐resolved serial femtosecond crystallography (SFX) and solution scattering techniques enable direct visualisation of early chemical change in light‐activated proteins on timescales previously inaccessible, whereas scattering gives access to slower timescales associated with more global structural change. Here, we review how advances in time‐resolved SFX and solution scattering techniques have uncovered mechanisms of photochemistry and its coupling to output responses. We also provide a prospective on how these time‐resolved structural approaches might impact on other photoreceptors/photoenzymes that have not yet been studied by these methods.
Keywords	X-radiation ; absorption ; crystallography ; energy ; harness ; photocatalysts ; photochemistry ; photons ; photoreceptors ; reaction chemistry
Language	English
Dates of publication	2022-02
Size	p. 576-595.
Publishing place	John Wiley & Sons, Ltd
Document type	Article
Note	REVIEW
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.15880
Database	NAL-Catalogue (AGRICOLA)

In stock of ZB MED Bonn / Germany

Z 2006/704: Show issues

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Solution-State Inter-Copper Distribution of Redox Partner-Linked Copper Nitrite Reductases: A Pulsed Electron-Electron Double Resonance Spectroscopy Study.

Hedison, Tobias M / Iorgu, Andreea I / Calabrese, Donato / Heyes, Derren J / Shanmugam, Muralidharan / Scrutton, Nigel S

The journal of physical chemistry letters

2022 Volume 13, Issue 30, Page(s) 6927–6934

Abstract: Copper nitrite reductases (CuNiRs) catalyze the reduction of nitrite to form nitric oxide. In recent years, new classes of redox partner linked CuNiRs have been isolated and characterized by crystallographic techniques. Solution-state biophysical studies ...

Abstract	Copper nitrite reductases (CuNiRs) catalyze the reduction of nitrite to form nitric oxide. In recent years, new classes of redox partner linked CuNiRs have been isolated and characterized by crystallographic techniques. Solution-state biophysical studies have shed light on the complex catalytic mechanisms of these enzymes and implied that protein dynamics may play a role in CuNiR catalysis. To investigate the structural, dynamical, and functional relationship of these CuNiRs, we have used protein reverse engineering and pulsed electron-electron double resonance (PELDOR) spectroscopy to determine their solution-state inter-copper distributions. Data show the multidimensional conformational landscape of this family of enzymes and the role of tethering in catalysis. The importance of combining high-resolution crystallographic techniques and low-resolution solution-state approaches in determining the structures and mechanisms of metalloenzymes is emphasized by our approach.
MeSH term(s)	Copper/chemistry ; Electrons ; Nitrite Reductases/chemistry ; Nitrite Reductases/metabolism ; Oxidation-Reduction ; Spectrum Analysis
Chemical Substances	Copper (789U1901C5) ; Nitrite Reductases (EC 1.7.-)
Language	English
Publishing date	2022-07-22
Publishing country	United States
Document type	Journal Article
ISSN	1948-7185
ISSN (online)	1948-7185
DOI	10.1021/acs.jpclett.2c01584
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: An unusual light-sensing function for coenzyme B

Poddar, Harshwardhan / Heyes, Derren J / Zhang, Shaowei / Hardman, Samantha J / Sakuma, Michiyo / Scrutton, Nigel S

Methods in enzymology

2022 Volume 668, Page(s) 349–372

Abstract: ... Coenzyme ... ...

Abstract	Coenzyme B
MeSH term(s)	Bacterial Proteins/metabolism ; Cobamides/chemistry ; Cobamides/genetics ; Cobamides/metabolism ; DNA/metabolism ; Gene Expression Regulation, Bacterial ; Phosphothreonine/analogs & derivatives ; Thermus thermophilus/genetics ; Thermus thermophilus/metabolism ; Vitamin B 12/metabolism
Chemical Substances	Bacterial Proteins ; Cobamides ; 7-mercaptoheptanoylthreonine phosphate (104302-77-4) ; Phosphothreonine (1114-81-4) ; DNA (9007-49-2) ; Vitamin B 12 (P6YC3EG204)
Language	English
Publishing date	2022-01-28
Publishing country	United States
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ISSN	1557-7988
ISSN (online)	1557-7988
DOI	10.1016/bs.mie.2021.12.010
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Photoinduced Electron Transfer from a 1,4,5,6-Tetrahydro Nicotinamide Adenine Dinucleotide (Phosphate) Analogue to Oxidized Flavin in an Ene-Reductase Flavoenzyme.

Speirs, Magnus / Hardman, Samantha J O / Iorgu, Andreea I / Johannissen, Linus O / Heyes, Derren J / Scrutton, Nigel S / Sazanovich, Igor V / Hay, Sam

The journal of physical chemistry letters

2023 Volume 14, Issue 13, Page(s) 3236–3242

Abstract: Recent reports have described the use of ene-reductase flavoenzymes to catalyze non-natural photochemical reactions. These studies have focused on using reduced flavoenzyme, yet oxidized flavins have superior light harvesting properties. In a binary ... ...

Abstract	Recent reports have described the use of ene-reductase flavoenzymes to catalyze non-natural photochemical reactions. These studies have focused on using reduced flavoenzyme, yet oxidized flavins have superior light harvesting properties. In a binary complex of the oxidized ene-reductase pentaerythritol tetranitrate reductase with the nonreactive nicotinamide coenzyme analogs 1,4,5,6-tetrahydro NAD(P)H, visible photoexcitation of the flavin mononucleotide (FMN) leads to one-electron transfer from the NAD(P)H
MeSH term(s)	Oxidoreductases/chemistry ; NAD/chemistry ; NADP ; Oxidation-Reduction ; Electrons ; Flavins/chemistry ; Phosphates ; Kinetics
Chemical Substances	Oxidoreductases (EC 1.-) ; NAD (0U46U6E8UK) ; NADP (53-59-8) ; Flavins ; Phosphates
Language	English
Publishing date	2023-03-27
Publishing country	United States
Document type	Journal Article
ISSN	1948-7185
ISSN (online)	1948-7185
DOI	10.1021/acs.jpclett.3c00176
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article: Advantages of brain penetrating inhibitors of kynurenine-3-monooxygenase for treatment of neurodegenerative diseases

Zhang, Shaowei / Collier, Mary E.W / Heyes, Derren J / Giorgini, Flaviano / Scrutton, Nigel S

Archives of biochemistry and biophysics. 2021 Jan. 15, v. 697

2021

Abstract: Kynurenine-3-monooxygenase (KMO) is an important therapeutic target for several brain disorders that has been extensively studied in recent years. Potent inhibitors towards KMO have been developed and tested within different disease models, showing great ...

Abstract	Kynurenine-3-monooxygenase (KMO) is an important therapeutic target for several brain disorders that has been extensively studied in recent years. Potent inhibitors towards KMO have been developed and tested within different disease models, showing great therapeutic potential, especially in models of neurodegenerative disease. The inhibition of KMO reduces the production of downstream toxic kynurenine pathway metabolites and shifts the flux to the formation of the neuroprotectant kynurenic acid. However, the efficacy of KMO inhibitors in neurodegenerative disease has been limited by their poor brain permeability. Combined with virtual screening and prodrug strategies, a novel brain penetrating KMO inhibitor has been developed which dramatically decreases neurotoxic metabolites. This review highlights the importance of KMO as a drug target in neurological disease and the benefits of brain permeable inhibitors in modulating kynurenine pathway metabolites in the central nervous system.
Keywords	biophysics ; brain ; drugs ; kynurenine pathway ; metabolites ; neurodegenerative diseases ; neurotoxicity ; permeability ; therapeutics
Language	English
Dates of publication	2021-0115
Publishing place	Elsevier Inc.
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	523-x
ISSN	1096-0384 ; 0003-9861
ISSN (online)	1096-0384
ISSN	0003-9861
DOI	10.1016/j.abb.2020.108702
Database	NAL-Catalogue (AGRICOLA)

In stock of ZB MED Bonn / Germany

Z 4' 70/107: Show issues
Archiv: Show issues

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: A guide to time-resolved structural analysis of light-activated proteins.

Poddar, Harshwardhan / Heyes, Derren J / Schirò, Giorgio / Weik, Martin / Leys, David / Scrutton, Nigel S

The FEBS journal

2021 Volume 289, Issue 3, Page(s) 576–595

Abstract: Dynamical changes in protein structures are essential for protein function and occur over femtoseconds to seconds timescales. X-ray free electron lasers have facilitated investigations of structural dynamics in proteins with unprecedented temporal and ... ...

Abstract	Dynamical changes in protein structures are essential for protein function and occur over femtoseconds to seconds timescales. X-ray free electron lasers have facilitated investigations of structural dynamics in proteins with unprecedented temporal and spatial resolution. Light-activated proteins are attractive targets for time-resolved structural studies, as the reaction chemistry and associated protein structural changes can be triggered by short laser pulses. Proteins with different light-absorbing centres have evolved to detect light and harness photon energy to bring about downstream chemical and biological output responses. Following light absorption, rapid chemical/small-scale structural changes are typically localised around the chromophore. These localised changes are followed by larger structural changes propagated throughout the photoreceptor/photocatalyst that enables the desired chemical and/or biological output response. Time-resolved serial femtosecond crystallography (SFX) and solution scattering techniques enable direct visualisation of early chemical change in light-activated proteins on timescales previously inaccessible, whereas scattering gives access to slower timescales associated with more global structural change. Here, we review how advances in time-resolved SFX and solution scattering techniques have uncovered mechanisms of photochemistry and its coupling to output responses. We also provide a prospective on how these time-resolved structural approaches might impact on other photoreceptors/photoenzymes that have not yet been studied by these methods.
MeSH term(s)	Crystallography, X-Ray ; Lasers ; Light ; Models, Molecular ; Protein Conformation/radiation effects ; Proteins/chemistry ; Proteins/radiation effects ; Proteins/ultrastructure ; Time Factors ; X-Ray Diffraction
Chemical Substances	Proteins
Language	English
Publishing date	2021-05-01
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.15880
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 260: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: How Photoactivation Triggers Protochlorophyllide Reduction: Computational Evidence of a Stepwise Hydride Transfer during Chlorophyll Biosynthesis.

Johannissen, Linus O / Taylor, Aoife / Hardman, Samantha J O / Heyes, Derren J / Scrutton, Nigel S / Hay, Sam

ACS catalysis

2022 Volume 12, Issue 7, Page(s) 4141–4148

Abstract: The photochemical reaction catalyzed by enzyme protochlorophyllide oxidoreductase (POR), a rare example of a photoactivated enzyme, is a crucial step during chlorophyll biosynthesis and involves the fastest known biological hydride transfer. Structures ... ...

Abstract	The photochemical reaction catalyzed by enzyme protochlorophyllide oxidoreductase (POR), a rare example of a photoactivated enzyme, is a crucial step during chlorophyll biosynthesis and involves the fastest known biological hydride transfer. Structures of the enzyme with bound substrate protochlorophyllide (PChlide) and coenzyme nicotinamide adenine dinucleotide phosphate (NADPH) have recently been published, opening up the possibility of using computational approaches to provide a comprehensive understanding of the excited state chemistry. Herein, we propose a complete mechanism for the photochemistry between PChlide and NADPH based on density functional theory (DFT) and time-dependent DFT calculations that is consistent with recent experimental data. In this multi-step mechanism, photoexcitation of PChlide leads to electron transfer from NADPH to PChlide, which in turn facilitates hydrogen atom transfer by weakening the breaking C-H bond. This work rationalizes how photoexcitation facilitates hydride transfer in POR and has more general implications for biological hydride transfer reactions.
Language	English
Publishing date	2022-03-21
Publishing country	United States
Document type	Journal Article
ISSN	2155-5435
ISSN	2155-5435
DOI	10.1021/acscatal.2c00866
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: Photocobilins integrate B

Zhang, Shaowei / Jeffreys, Laura N / Poddar, Harshwardhan / Yu, Yuqi / Liu, Chuanyang / Patel, Kaylee / Johannissen, Linus O / Zhu, Lingyun / Cliff, Matthew J / Yan, Cunyu / Schirò, Giorgio / Weik, Martin / Sakuma, Michiyo / Levy, Colin W / Leys, David / Heyes, Derren J / Scrutton, Nigel S

Nature communications

2024 Volume 15, Issue 1, Page(s) 2740

Abstract: Photoreceptor proteins utilise chromophores to sense light and trigger a biological response. The discovery that adenosylcobalamin (or coenzyme ... ...

Abstract	Photoreceptor proteins utilise chromophores to sense light and trigger a biological response. The discovery that adenosylcobalamin (or coenzyme B
MeSH term(s)	Photochemistry ; Bile Pigments ; Biliverdine ; Bacterial Proteins/metabolism ; Photoreceptors, Microbial/chemistry ; Light
Chemical Substances	Bile Pigments ; Biliverdine (O9MIA842K9) ; Bacterial Proteins ; Photoreceptors, Microbial
Language	English
Publishing date	2024-03-28
Publishing country	England
Document type	Journal Article
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-024-46995-1
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article: Kinetic characterisation of Erv1, a key component for protein import and folding in yeast mitochondria

Tang, Xiaofan / Ang, Swee Kim / Ceh‐Pavia, Efrain / Heyes, Derren J / Lu, Hui

FEBS journal. 2020 Mar., v. 287, no. 6

2020

Abstract: Yeast (Saccharomyces cerevisiae) essential for respiration and viability 1 (Erv1; EC number 1.8.3.2), a member of the flavin adenine dinucleotide‐dependent Erv1/ALR disulphide bond generating enzyme family, works together with Mia40 to catalyse protein ... ...

Abstract	Yeast (Saccharomyces cerevisiae) essential for respiration and viability 1 (Erv1; EC number 1.8.3.2), a member of the flavin adenine dinucleotide‐dependent Erv1/ALR disulphide bond generating enzyme family, works together with Mia40 to catalyse protein import and oxidative folding in the mitochondrial intermembrane space. Erv1/ALR functions either as an oxidase or cytochrome c reductase by passing electrons from a thiol substrate to molecular oxygen (O₂) or cytochrome c, respectively. However, the substrate specificity for oxygen and cytochrome c is not fully understood. In this study, the oxidase and cytochrome c reductase kinetics of yeast Erv1 were investigated in detail, under aerobic and anaerobic conditions, using stopped‐flow absorption spectroscopy and oxygen consumption analysis. Using DTT as an electron donor, our results show that cytochrome c is ~ 7‐ to 15‐fold more efficient than O₂ as electron acceptors for yeast Erv1, and that O₂ is a competitive inhibitor of Erv1 cytochrome c reductase activity. In addition, Mia40, the physiological thiol substrate of Erv1, was used as an electron donor for Erv1 in a detailed enzyme kinetic study. Different enzyme kinetic kcₐₜ and Kₘ values were obtained with Mia40 compared to DTT, suggesting that Mia40 modulates Erv1 enzyme kinetics. Taken together, this study shows that Erv1 is a moderately active enzyme with the ability to use both O₂ and cytochrome c as the electron acceptors, indicating that Erv1 contributes to mitochondrial hydrogen peroxide production. Our results also suggest that Mia40‐Erv1 system may involve in regulation of the redox state of glutathione in the mitochondrial intermembrane space. ERV1: EC number 1.8.3.2.
Keywords	Saccharomyces cerevisiae ; adenine ; disulfide bonds ; enzyme kinetics ; glutathione ; hydrogen peroxide ; mitochondria ; oxygen ; oxygen consumption ; protein transport ; spectroscopy ; substrate specificity ; thiols ; viability ; yeasts
Language	English
Dates of publication	2020-03
Size	p. 1220-1231.
Publishing place	John Wiley & Sons, Ltd
Document type	Article
Note	NAL-AP-2-clean ; JOURNAL ARTICLE
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.15077
Database	NAL-Catalogue (AGRICOLA)

In stock of ZB MED Bonn / Germany

Z 2006/704: Show issues

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾
- See ZB MED holdings
- Order with fees

To top

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED