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Understanding Photochemical N2 Reduction Using CdS Quantum Dot MoFe Protein Biohybrids
Understanding Photochemical N2 Reduction Using CdS Quantum Dot MoFe Protein Biohybrids
상세정보
- 자료유형
- 학위논문 서양
- 최종처리일시
- 20250211152702
- ISBN
- 9798384051848
- DDC
- 541
- 서명/저자
- Understanding Photochemical N2 Reduction Using CdS Quantum Dot MoFe Protein Biohybrids
- 발행사항
- [Sl] : University of Colorado at Boulder, 2024
- 발행사항
- Ann Arbor : ProQuest Dissertations & Theses, 2024
- 형태사항
- 170 p
- 주기사항
- Source: Dissertations Abstracts International, Volume: 86-03, Section: B.
- 주기사항
- Advisor: Dukovic, Gordana.
- 학위논문주기
- Thesis (Ph.D.)--University of Colorado at Boulder, 2024.
- 초록/해제
- 요약Due to increases in greenhouse gas emissions from large scale industrial processes, such as the Haber-Bosch process, the world is dealing with increases in global temperatures. Researching new ways to use renewable sources such as solar energy can help us understand new ways to move away from fossil fuels. One emerging way to study photocatalysis is through semiconductor nanocrystal (NC) biohybrids. In these systems, semiconductor NCs are directly coupled to redox enzymes to drive photochemistry. This work focuses on the study of CdS quantum dots (QDs) to the MoFe protein of the nitrogenase enzyme for light driven N2 reduction. By replacing the native electron donor and directly coupling CdS QDs to the MoFe protein of the nitrogenase enzyme photocatalytic N2 reduction can be achieved. The coupling of CdS QD to the MoFe protein is an important factor for interfacial electron transfer from CdS QDs to the MoFe protein. To characterize this binding interaction, microscale thermophoresis was developed for CdS QD - MoFe protein systems. This technique revealed that the interaction between CdS QDs and the MoFe protein is strong, primarily driven by electrostatics, and sensitive to the CdS QD diameter. To better understand the photocatalytic mechanism of N2 reduction light, the sequential electron transfer from the CdS QDs into the MoFe protein's active site was studied using EPR spectroscopy giving information on how catalytic intermediates evolve over time. Finally, the impact of the surface-capping ligand was studied to understand how CdS QD properties affect photochemical N2 reduction in CdS QD - MoFe protein systems. It was found that changing the surface capping ligand increased the rate of NH3 product formation. Electron transfer from the long-lived electrons to the MoFe protein is hypothesized to contribute to the increase in the rate NH3 product formation, increasing the quantum efficiency of electron transfer. This dissertation illustrates a fundamental understanding of CdS QD - MoFe protein systems through a combination of different experimental techniques.
- 일반주제명
- Physical chemistry
- 일반주제명
- Chemistry
- 일반주제명
- Nanoscience
- 키워드
- MoFe protein
- 키워드
- Nitrogenase
- 키워드
- Quantum dots
- 기타저자
- University of Colorado at Boulder Chemistry
- 기본자료저록
- Dissertations Abstracts International. 86-03B.
- 전자적 위치 및 접속
- 로그인 후 원문을 볼 수 있습니다.
MARC
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■00520250211152702
■006m o d
■007cr#unu||||||||
■020 ▼a9798384051848
■035 ▼a(MiAaPQ)AAI31488063
■040 ▼aMiAaPQ▼cMiAaPQ
■0820 ▼a541
■1001 ▼aPellows, Lauren M.▼0(orcid)0000-0002-1088-1898
■24510▼aUnderstanding Photochemical N2 Reduction Using CdS Quantum Dot MoFe Protein Biohybrids
■260 ▼a[Sl]▼bUniversity of Colorado at Boulder▼c2024
■260 1▼aAnn Arbor▼bProQuest Dissertations & Theses▼c2024
■300 ▼a170 p
■500 ▼aSource: Dissertations Abstracts International, Volume: 86-03, Section: B.
■500 ▼aAdvisor: Dukovic, Gordana.
■5021 ▼aThesis (Ph.D.)--University of Colorado at Boulder, 2024.
■520 ▼aDue to increases in greenhouse gas emissions from large scale industrial processes, such as the Haber-Bosch process, the world is dealing with increases in global temperatures. Researching new ways to use renewable sources such as solar energy can help us understand new ways to move away from fossil fuels. One emerging way to study photocatalysis is through semiconductor nanocrystal (NC) biohybrids. In these systems, semiconductor NCs are directly coupled to redox enzymes to drive photochemistry. This work focuses on the study of CdS quantum dots (QDs) to the MoFe protein of the nitrogenase enzyme for light driven N2 reduction. By replacing the native electron donor and directly coupling CdS QDs to the MoFe protein of the nitrogenase enzyme photocatalytic N2 reduction can be achieved. The coupling of CdS QD to the MoFe protein is an important factor for interfacial electron transfer from CdS QDs to the MoFe protein. To characterize this binding interaction, microscale thermophoresis was developed for CdS QD - MoFe protein systems. This technique revealed that the interaction between CdS QDs and the MoFe protein is strong, primarily driven by electrostatics, and sensitive to the CdS QD diameter. To better understand the photocatalytic mechanism of N2 reduction light, the sequential electron transfer from the CdS QDs into the MoFe protein's active site was studied using EPR spectroscopy giving information on how catalytic intermediates evolve over time. Finally, the impact of the surface-capping ligand was studied to understand how CdS QD properties affect photochemical N2 reduction in CdS QD - MoFe protein systems. It was found that changing the surface capping ligand increased the rate of NH3 product formation. Electron transfer from the long-lived electrons to the MoFe protein is hypothesized to contribute to the increase in the rate NH3 product formation, increasing the quantum efficiency of electron transfer. This dissertation illustrates a fundamental understanding of CdS QD - MoFe protein systems through a combination of different experimental techniques.
■590 ▼aSchool code: 0051.
■650 4▼aPhysical chemistry
■650 4▼aChemistry
■650 4▼aNanoscience
■653 ▼aElectron paramagnetic resonance
■653 ▼aMicroscale thermophoresis
■653 ▼aMoFe protein
■653 ▼aNitrogenase
■653 ▼aQuantum dots
■653 ▼aTransient absorption spectroscopy
■690 ▼a0494
■690 ▼a0565
■690 ▼a0485
■71020▼aUniversity of Colorado at Boulder▼bChemistry.
■7730 ▼tDissertations Abstracts International▼g86-03B.
■790 ▼a0051
■791 ▼aPh.D.
■792 ▼a2024
■793 ▼aEnglish
■85640▼uhttp://www.riss.kr/pdu/ddodLink.do?id=T17163391▼nKERIS▼z이 자료의 원문은 한국교육학술정보원에서 제공합니다.
