{"id":{"repo_id":"east-anglia","oai_identifier":"oai:ueaeprints.uea.ac.uk:52053"},"canonical_url":"https://search.dev.ndltd.org/etd/east-anglia/oai:ueaeprints.uea.ac.uk:52053","repository":{"repo_id":"east-anglia","name":"University of East Anglia","base_url":"https://ueaeprints.uea.ac.uk/cgi/oai2"},"display":{"title":"Understanding the [Fe Fe]-Hydrogenase H-Cluster: Insights From Chemical Modelling and Advanced Spectroscopy","abstract":"Hydrogenase enzymes are nature’s catalysts for hydrogen production and uptake. Understanding how they work may lead to new materials as alternatives for precious metals currently used in H2-utilizing fuel and producer cells. Work described in this thesis focuses on synthetic mimics of the active site of [Fe Fe]-hydrogenases and explores their reactivity towards protons and electrons. Chapter 1 gives a brief overview of the chemistry taking place in hydogenase enzymes with a particular focus on the [Fe Fe]-hydrogenase. The evolution of synthetic models mimicking the structure and function of the enzyme from the late 1990s to the current state of the art is discussed. Chapter 2 describes synthesis of the first {2Fe3S} hydride together with new active site mimics in which bulky substituents are incorporated into the dithiolate bridgehead. A comprehensive examination of their structural features and spectroscopic properties is provided. Chapter 3 reports extensive stopped-flow UV-vis, IR and electrochemical studies for a range of subsite models exploring the relationship between the structure and the reactivity towards protons. It is shown that there is a direct linear free energy relationship between the activation energy for protonation and the energy level of the HOMO. Chapter 4 describes the first characterisation of paramagnetic (mixed-valence) Fe(I)(μ-H)- Fe(II) species which is implicated in metallo-sulfur enzymes as an intermediate in electrocatalytic H2 evolution. An unprecedented super reduced state is detected and characterised using a custom-built spectroelectrochemical cell.Chapter 5 shows how muon spectroscopy may provide a new approach for exploring metallo-hydride chemistry. Future avenues of research in the field of [Fe Fe] chemistry arising from the work described in this thesis are also briefly discussed.","abstract_html":"Hydrogenase enzymes are nature’s catalysts for hydrogen production and uptake. Understanding how they work may lead to new materials as alternatives for precious metals currently used in H2-utilizing fuel and producer cells. Work described in this thesis focuses on synthetic mimics of the active site of [Fe Fe]-hydrogenases and explores their reactivity towards protons and electrons. Chapter 1 gives a brief overview of the chemistry taking place in hydogenase enzymes with a particular focus on the [Fe Fe]-hydrogenase. The evolution of synthetic models mimicking the structure and function of the enzyme from the late 1990s to the current state of the art is discussed. Chapter 2 describes synthesis of the first {2Fe3S} hydride together with new active site mimics in which bulky substituents are incorporated into the dithiolate bridgehead. A comprehensive examination of their structural features and spectroscopic properties is provided. Chapter 3 reports extensive stopped-flow UV-vis, IR and electrochemical studies for a range of subsite models exploring the relationship between the structure and the reactivity towards protons. It is shown that there is a direct linear free energy relationship between the activation energy for protonation and the energy level of the HOMO. Chapter 4 describes the first characterisation of paramagnetic (mixed-valence) Fe(I)(μ-H)- Fe(II) species which is implicated in metallo-sulfur enzymes as an intermediate in electrocatalytic H2 evolution. An unprecedented super reduced state is detected and characterised using a custom-built spectroelectrochemical cell.Chapter 5 shows how muon spectroscopy may provide a new approach for exploring metallo-hydride chemistry. Future avenues of research in the field of [Fe Fe] chemistry arising from the work described in this thesis are also briefly discussed.","abstract_has_math":false,"creators":["Jablonskyte, Ausra"],"institution":"University of East Anglia","degree_name":"phd","degree_level":"doctoral","degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2014,"date_issued":"2014-06","date_published":"2014-06","updated_at":"2026-07-24T02:12:06Z","subjects":[],"languages":["en"],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":null,"outbound_label":null,"outbound_source":null},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["Jablonskyte, Ausra"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2014-06"]},{"key":"dc:date.issued","label":"Date","values":["2014-06"]},{"key":"dc:publisher.department","label":"Dc Publisher Department","values":["School of Chemistry"]},{"key":"dc:publisher.institution","label":"Dc Publisher Institution","values":["University of East Anglia"]},{"key":"dc:relation.isreferencedby","label":"Dc Relation Isreferencedby","values":["https://ueaeprints.uea.ac.uk/id/eprint/52053/"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]},{"key":"dc:type.qualificationlevel","label":"Dc Type Qualificationlevel","values":["doctoral"]},{"key":"dc:type.qualificationname","label":"Dc Type Qualificationname","values":["phd"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["en"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://ueaeprints.uea.ac.uk/id/eprint/52053/1/2014JablonskyteA_-_Thesis.pdf"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Hydrogenase enzymes are nature’s catalysts for hydrogen production and uptake. Understanding how they work may lead to new materials as alternatives for precious metals currently used in H2-utilizing fuel and producer cells. Work described in this thesis focuses on synthetic mimics of the active site of [Fe Fe]-hydrogenases and explores their reactivity towards protons and electrons. Chapter 1 gives a brief overview of the chemistry taking place in hydogenase enzymes with a particular focus on the [Fe Fe]-hydrogenase. The evolution of synthetic models mimicking the structure and function of the enzyme from the late 1990s to the current state of the art is discussed. Chapter 2 describes synthesis of the first {2Fe3S} hydride together with new active site mimics in which bulky substituents are incorporated into the dithiolate bridgehead. A comprehensive examination of their structural features and spectroscopic properties is provided. Chapter 3 reports extensive stopped-flow UV-vis, IR and electrochemical studies for a range of subsite models exploring the relationship between the structure and the reactivity towards protons. It is shown that there is a direct linear free energy relationship between the activation energy for protonation and the energy level of the HOMO. Chapter 4 describes the first characterisation of paramagnetic (mixed-valence) Fe(I)(μ-H)- Fe(II) species which is implicated in metallo-sulfur enzymes as an intermediate in electrocatalytic H2 evolution. An unprecedented super reduced state is detected and characterised using a custom-built spectroelectrochemical cell.Chapter 5 shows how muon spectroscopy may provide a new approach for exploring metallo-hydride chemistry. Future avenues of research in the field of [Fe Fe] chemistry arising from the work described in this thesis are also briefly discussed."]},{"key":"dc:format","label":"Dc Format","values":["application/pdf"]},{"key":"dc:title","label":"Title","values":["Understanding the [Fe Fe]-Hydrogenase H-Cluster: Insights From Chemical Modelling and Advanced Spectroscopy"]}]}],"canonical_facts":{"dc:creator":["Jablonskyte, Ausra"],"dc:date":["2014-06"],"dc:date.issued":["2014-06"],"dc:description.abstract":["Hydrogenase enzymes are nature’s catalysts for hydrogen production and uptake. Understanding how they work may lead to new materials as alternatives for precious metals currently used in H2-utilizing fuel and producer cells. Work described in this thesis focuses on synthetic mimics of the active site of [Fe Fe]-hydrogenases and explores their reactivity towards protons and electrons. Chapter 1 gives a brief overview of the chemistry taking place in hydogenase enzymes with a particular focus on the [Fe Fe]-hydrogenase. The evolution of synthetic models mimicking the structure and function of the enzyme from the late 1990s to the current state of the art is discussed. Chapter 2 describes synthesis of the first {2Fe3S} hydride together with new active site mimics in which bulky substituents are incorporated into the dithiolate bridgehead. A comprehensive examination of their structural features and spectroscopic properties is provided. Chapter 3 reports extensive stopped-flow UV-vis, IR and electrochemical studies for a range of subsite models exploring the relationship between the structure and the reactivity towards protons. It is shown that there is a direct linear free energy relationship between the activation energy for protonation and the energy level of the HOMO. Chapter 4 describes the first characterisation of paramagnetic (mixed-valence) Fe(I)(μ-H)- Fe(II) species which is implicated in metallo-sulfur enzymes as an intermediate in electrocatalytic H2 evolution. An unprecedented super reduced state is detected and characterised using a custom-built spectroelectrochemical cell.Chapter 5 shows how muon spectroscopy may provide a new approach for exploring metallo-hydride chemistry. Future avenues of research in the field of [Fe Fe] chemistry arising from the work described in this thesis are also briefly discussed."],"dc:format":["application/pdf"],"dc:identifier.uri":["https://ueaeprints.uea.ac.uk/id/eprint/52053/1/2014JablonskyteA_-_Thesis.pdf"],"dc:language":["en"],"dc:publisher.department":["School of Chemistry"],"dc:publisher.institution":["University of East Anglia"],"dc:relation.isreferencedby":["https://ueaeprints.uea.ac.uk/id/eprint/52053/"],"dc:title":["Understanding the [Fe Fe]-Hydrogenase H-Cluster: Insights From Chemical Modelling and Advanced Spectroscopy"],"dc:type":["Thesis"],"dc:type.qualificationlevel":["doctoral"],"dc:type.qualificationname":["phd"]},"updated_at":"2026-07-24T02:12:06Z"}