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Article ; Online: Featuring... Frank Sargent winner of the 2009 FEBS Letters Young Scientist Award. Interview by Daniela Ruffell.

Sargent, Frank

2009 Volume 583, Issue 11, Page(s) 1654–1655

MeSH term(s)	Awards and Prizes ; Escherichia coli Proteins/metabolism ; Escherichia coli Proteins/physiology ; History, 21st Century ; Humans ; Membrane Transport Proteins/metabolism ; Membrane Transport Proteins/physiology ; Scotland
Chemical Substances	Escherichia coli Proteins ; Membrane Transport Proteins ; twin-arginine translocase complex, E coli
Language	English
Publishing date	2009-06-05
Publishing country	England
Document type	Biography ; Historical Article ; Interview
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1016/j.febslet.2009.04.034
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Article ; Online: Formate hydrogenlyase, formic acid translocation and hydrogen production: dynamic membrane biology during fermentation.

Peters, Katharina / Sargent, Frank

Biochimica et biophysica acta. Bioenergetics

2022 Volume 1864, Issue 1, Page(s) 148919

Abstract: Formate hydrogenlyase-1 (FHL-1) is a complex-I-like enzyme that is commonly found in gram-negative bacteria. The enzyme comprises a peripheral arm and a membrane arm but is not involved in quinone reduction. Instead, FHL-1 couples formate oxidation to ... ...

Abstract	Formate hydrogenlyase-1 (FHL-1) is a complex-I-like enzyme that is commonly found in gram-negative bacteria. The enzyme comprises a peripheral arm and a membrane arm but is not involved in quinone reduction. Instead, FHL-1 couples formate oxidation to the reduction of protons to molecular hydrogen (H
MeSH term(s)	Escherichia coli ; Fermentation ; Formate Dehydrogenases/chemistry ; Formates/chemistry ; Hydrogen
Chemical Substances	Formate Dehydrogenases (EC 1.17.1.9) ; Formates ; formic acid (0YIW783RG1) ; Hydrogen (7YNJ3PO35Z)
Language	English
Publishing date	2022-09-21
Publishing country	Netherlands
Document type	Review ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2650 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2650 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbabio.2022.148919
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Article ; Online: A paean to the ineffable Marjory Stephenson.

Sargent, Frank / Sawers, R Gary

Microbiology (Reading, England)

2022 Volume 168, Issue 3

Abstract: It is now 75 years since Marjory Stephenson became the second President of the Society for General Microbiology (SGM). Around the time of her death at the end of 1948 many articles appeared extolling Marjory Stephenson's contribution to the fields of ... ...

Abstract	It is now 75 years since Marjory Stephenson became the second President of the Society for General Microbiology (SGM). Around the time of her death at the end of 1948 many articles appeared extolling Marjory Stephenson's contribution to the fields of Biochemistry and Microbiology. Not that much has been written about her since that time, which is unfortunate. Therefore, this brief review is intended as a form of redress and aims to highlight the role of this remarkable scientist in establishing the Society and in promoting Microbiology as a discipline. Notwithstanding the significance of these achievements, however, it is her overall impact on the field of 'Chemical Microbiology' and what she achieved through her research that are extraordinary, even by today's standards. Marjory Stephenson recognized that in order to understand a biological system, the 'whole' organism must be considered and this can only be achieved by adopting an interdisciplinary approach: inorganic and organic chemistry, biochemistry, genetics, metabolism and ultimately physiology. Her scientific ethos serves today as a beacon for how scientific research should be conducted, and what we as scientists can learn about how to inspire and mentor the next generation. It is impossible to overstate Marjory Stephenson's scientific legacy, or her overall contribution to Microbiology.
Language	English
Publishing date	2022-06-19
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1180712-x
ISSN	1465-2080 ; 1350-0872
ISSN (online)	1465-2080
ISSN	1350-0872
DOI	10.1099/mic.0.001160
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Article: Formate hydrogenlyase, formic acid translocation and hydrogen production: dynamic membrane biology during fermentation

Peters, Katharina / Sargent, Frank

Biochimica et biophysica acta. 2023 Jan. 01, v. 1864, no. 1

2023

Abstract	Formate hydrogenlyase-1 (FHL-1) is a complex-I-like enzyme that is commonly found in gram-negative bacteria. The enzyme comprises a peripheral arm and a membrane arm but is not involved in quinone reduction. Instead, FHL-1 couples formate oxidation to the reduction of protons to molecular hydrogen (H₂). Escherichia coli produces FHL-1 under fermentative conditions where it serves to detoxify formic acid in the environment. The membrane biology and bioenergetics surrounding E. coli FHL-1 have long held fascination. Here, we review recent work on understanding the molecular basis of formic acid efflux and influx. We also consider the structure and function of E. coli FHL-1, its relationship with formate transport, and pay particular attention to the molecular interface between the peripheral arm and the membrane arm. Finally, we highlight the interesting phenotype of genetic mutation of the ND1 Loop, which is located at that interface.
Keywords	Escherichia coli ; fermentation ; formate dehydrogenase ; formates ; formic acid ; hydrogen ; hydrogen production ; mutation ; oxidation ; phenotype ; quinones
Language	English
Dates of publication	2023-0101
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	282711-6
ISSN	0005-2728 ; 0304-4173
ISSN	0005-2728 ; 0304-4173
DOI	10.1016/j.bbabio.2022.148919
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Hydrogen production in the presence of oxygen by

Metcalfe, George D / Sargent, Frank / Hippler, Michael

Microbiology (Reading, England)

2022 Volume 168, Issue 3

Abstract: Escherichia ... ...

Abstract	Escherichia coli
MeSH term(s)	Escherichia coli/genetics ; Escherichia coli/metabolism ; Escherichia coli K12/genetics ; Escherichia coli K12/metabolism ; Escherichia coli Proteins/metabolism ; Hydrogen/metabolism ; Oxygen/metabolism
Chemical Substances	Escherichia coli Proteins ; Hydrogen (7YNJ3PO35Z) ; Oxygen (S88TT14065)
Language	English
Publishing date	2022-04-11
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1180712-x
ISSN	1465-2080 ; 1350-0872
ISSN (online)	1465-2080
ISSN	1350-0872
DOI	10.1099/mic.0.001167
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Article ; Online: Characterisation of anhydro-sialic acid transporters from mucosa-associated bacteria.

Wu, Yunhan / Bell, Andrew / Thomas, Gavin H / Bolam, David N / Sargent, Frank / Juge, Nathalie / Palmer, Tracy / Severi, Emmanuele

Microbiology (Reading, England)

2024 Volume 170, Issue 3

Abstract: Sialic acid (Sia) transporters are critical to the capacity of host-associated bacteria to utilise Sia for growth and/or cell surface modification. While N-acetyl-neuraminic acid (Neu5Ac)-specific transporters have been studied extensively, little is ... ...

Abstract	Sialic acid (Sia) transporters are critical to the capacity of host-associated bacteria to utilise Sia for growth and/or cell surface modification. While N-acetyl-neuraminic acid (Neu5Ac)-specific transporters have been studied extensively, little is known on transporters dedicated to anhydro-Sia forms such as 2,7-anhydro-Neu5Ac (2,7-AN) or 2,3-dehydro-2-deoxy-Neu5Ac (Neu5Ac2en). Here, we used a Sia-transport-null strain of
MeSH term(s)	N-Acetylneuraminic Acid/chemistry ; N-Acetylneuraminic Acid/analogs & derivatives ; Symporters/genetics ; Symporters/metabolism ; Bacteria/metabolism ; Membrane Transport Proteins/genetics ; Membrane Transport Proteins/metabolism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Organic Anion Transporters
Chemical Substances	2-deoxy-2,3-dehydro-N-acetylneuraminic acid (24967-27-9) ; sialic acid transport proteins ; N-Acetylneuraminic Acid (GZP2782OP0) ; Symporters ; Membrane Transport Proteins ; Organic Anion Transporters
Language	English
Publishing date	2024-03-15
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1180712-x
ISSN	1465-2080 ; 1350-0872
ISSN (online)	1465-2080
ISSN	1350-0872
DOI	10.1099/mic.0.001448
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Article ; Online: Harnessing Escherichia coli for Bio-Based Production of Formate under Pressurized H

Roger, Magali / Reed, Thomas C P / Sargent, Frank

Applied and environmental microbiology

2021 Volume 87, Issue 21, Page(s) e0029921

Abstract: Escherichia coli is a Gram-negative bacterium that is a workhorse for biotechnology. The organism naturally performs a mixed-acid fermentation under anaerobic conditions where it synthesizes formate hydrogenlyase (FHL-1). The physiological role of the ... ...

Abstract	Escherichia coli is a Gram-negative bacterium that is a workhorse for biotechnology. The organism naturally performs a mixed-acid fermentation under anaerobic conditions where it synthesizes formate hydrogenlyase (FHL-1). The physiological role of the enzyme is the disproportionation of formate into H
MeSH term(s)	Bioreactors ; Carbon Dioxide ; Deuterium ; Escherichia coli/genetics ; Formate Dehydrogenases/genetics ; Formates/metabolism ; Gases ; Molybdenum ; Tungsten
Chemical Substances	Formates ; Gases ; formic acid (0YIW783RG1) ; Carbon Dioxide (142M471B3J) ; Molybdenum (81AH48963U) ; Deuterium (AR09D82C7G) ; Formate Dehydrogenases (EC 1.17.1.9) ; Tungsten (V9306CXO6G)
Language	English
Publishing date	2021-09-08
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	223011-2
ISSN	1098-5336 ; 0099-2240
ISSN (online)	1098-5336
ISSN	0099-2240
DOI	10.1128/AEM.00299-21
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Article ; Online: A clinical approach to the investigation and management of long COVID associated neuropathic pain.

Shil, Rajish Sanjit Kumar / Hughes, Thomas William / Sargent, Brendan Francis / Huang, Yun / Tamborska, Arina Anna / Frank, Bernhard / Ellul, Mark Alexander / Michael, Benedict Daniel

European archives of psychiatry and clinical neuroscience

2023

Abstract: COVID-19 has been associated with a wide range of ongoing symptoms following recovery from the acute SARS-CoV-2 infection. Around one in three people with COVID-19 develop neurological symptoms with many reporting neuropathic pain and associated symptoms, ...

Abstract	COVID-19 has been associated with a wide range of ongoing symptoms following recovery from the acute SARS-CoV-2 infection. Around one in three people with COVID-19 develop neurological symptoms with many reporting neuropathic pain and associated symptoms, including paraesthesia, numbness, and dysesthesia. Whilst the pathophysiology of long COVID-19-associated neuropathic pain remains unclear, it is likely to be multifactorial. Early identification, exclusion of common alternative causes, and a biopsychosocial approach to the management of the symptoms can help in relieving the burden of disease and improving the quality of life for patients.
Language	English
Publishing date	2023-12-08
Publishing country	Germany
Document type	Journal Article ; Review
ZDB-ID	1045583-8
ISSN	1433-8491 ; 0175-758X ; 0940-1334
ISSN (online)	1433-8491
ISSN	0175-758X ; 0940-1334
DOI	10.1007/s00406-023-01721-8
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Article ; Online: Formate hydrogenlyase: A group 4 [NiFe]-hydrogenase in tandem with a formate dehydrogenase.

Finney, Alexander J / Sargent, Frank

Advances in microbial physiology

2019 Volume 74, Page(s) 465–486

Abstract: Hydrogenase enzymes are currently under the international research spotlight due to emphasis on biologically produced hydrogen as one potential energy carrier to relinquish the requirement for 'fossil fuel' derived energy. Three major classes of ... ...

Abstract	Hydrogenase enzymes are currently under the international research spotlight due to emphasis on biologically produced hydrogen as one potential energy carrier to relinquish the requirement for 'fossil fuel' derived energy. Three major classes of hydrogenase exist in microbes all able to catalyze the reversible oxidation of dihydrogen to protons and electrons. These classes are defined by their active site metal content: [NiFe]-; [FeFe]- and [Fe]-hydrogenases. Of these the [NiFe]-hydrogenases have links to ancient forms of metabolism, utilizing hydrogen as the original source of reductant on Earth. This review progresses to highlight the Group 4 [NiFe]-hydrogenase enzymes that preferentially generate hydrogen exploiting various partner enzymes or ferredoxin, while in some cases translocating ions across biological membranes. Specific focus is paid to Group 4A, the Formate hydrogenlyase complexes. These are the combination of a six or nine subunit [NiFe]-hydrogenase with a soluble formate dehydrogenase to derived electrons from formate oxidation for proton reduction. The incidence, physiology, structure and biotechnological application of these complexes will be explored with attention on Escherichia coli Formate Hydrogenlyase-1 (FHL-1).
MeSH term(s)	Biocatalysis ; Biotechnology ; Escherichia coli Proteins/chemistry ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; Formate Dehydrogenases/chemistry ; Formate Dehydrogenases/genetics ; Formate Dehydrogenases/metabolism ; Hydrogen/metabolism ; Hydrogenase/chemistry ; Hydrogenase/genetics ; Hydrogenase/metabolism ; Models, Molecular ; Multienzyme Complexes/chemistry ; Multienzyme Complexes/genetics ; Multienzyme Complexes/metabolism ; Operon ; Oxidation-Reduction
Chemical Substances	Escherichia coli Proteins ; Multienzyme Complexes ; Hydrogen (7YNJ3PO35Z) ; nickel-iron hydrogenase (EC 1.12.-) ; Hydrogenase (EC 1.12.7.2) ; Formate Dehydrogenases (EC 1.17.1.9) ; formate hydrogenlyase (EC 1.17.1.9)
Language	English
Publishing date	2019-02-28
Publishing country	England
Document type	Journal Article
ZDB-ID	174-0
ISSN	2162-5468 ; 0065-2911
ISSN (online)	2162-5468
ISSN	0065-2911
DOI	10.1016/bs.ampbs.2019.02.004
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Article ; Online: Erratum to 'Educational assessment of intrathoracic and extrathoracic surgical stabilization of rib fractures' [Injury volume 54 issue 1 (2023) pages 63-69].

Frank, Madelyn / Sargent, Brynn / Tay-Lasso, Erika / Hovis, Gabrielle / Kincaid, Colin / Grant, William / Alaniz, Leonardo / Yi, Justin / Chin, Theresa L / Barrios, Cristobal / Nahmias, Jeffry / Pieracci, Fredric / Schubl, Sebastian

Injury

2023 Volume 54, Issue 3, Page(s) 1024

Language	English
Publishing date	2023-02-01
Publishing country	Netherlands
Document type	Published Erratum
ZDB-ID	218778-4
ISSN	1879-0267 ; 0020-1383
ISSN (online)	1879-0267
ISSN	0020-1383
DOI	10.1016/j.injury.2023.01.022
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