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An Investigation Into Copper Proteins Germane to Biological Ammonia Oxidation
An Investigation Into Copper Proteins Germane to Biological Ammonia Oxidation
상세정보
- 자료유형
- 학위논문 서양
- 최종처리일시
- 20260202102955
- ISBN
- 9798283138442
- DDC
- 540
- 서명/저자
- An Investigation Into Copper Proteins Germane to Biological Ammonia Oxidation
- 발행사항
- [Sl] : Cornell University, 2025
- 발행사항
- Ann Arbor : ProQuest Dissertations & Theses, 2025
- 형태사항
- 122 p
- 주기사항
- Source: Dissertations Abstracts International, Volume: 86-12, Section: B.
- 주기사항
- Advisor: Lancaster, Kyle.
- 학위논문주기
- Thesis (Ph.D.)--Cornell University, 2025.
- 초록/해제
- 요약In lieu of carbon-based primary metabolisms found in plants and animals, certain bacteria and archaea survive by catabolizing ammonia. These organisms are globally pervasive and control biogeochemical nitrogen cycle fluxes. A dearth of understanding persists regarding the underlying biochemistry of these nitrogen-based metabolisms due to the difficulties associated with culturing ammonia-oxidizing organisms. Nevertheless, copper is known to play a vital role in biological ammonia oxidation (BAO).This thesis explores the biochemistry of two of the most abundant copper proteins in the model ammonia-oxidizing bacterium, Nitrosomonas europaea. Molecular biology and structural biology techniques are employed to develop a heterologous technology for the isolation of an integral membrane protein complex, which is believed to catalyze the first step of BAO, ammonia monooxygenase (AMO). Additionally, an investigation into the in vivo function of nitrosocyanin (Ncya) is made. Spectroscopic techniques are utilized to assess the activity and electron transfer kinetics of Ncya. The results provide insight into Ncya function and challenge proposed hypotheses.
- 일반주제명
- Chemistry
- 일반주제명
- Microbiology
- 일반주제명
- Biochemistry
- 키워드
- Nitrosocyanin
- 기타저자
- Cornell University Chemistry and Chemical Biology
- 기본자료저록
- Dissertations Abstracts International. 86-12B.
- 전자적 위치 및 접속
- 로그인 후 원문을 볼 수 있습니다.
MARC
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■020 ▼a9798283138442
■035 ▼a(MiAaPQ)AAI31768843
■040 ▼aMiAaPQ▼cMiAaPQ
■0820 ▼a540
■1001 ▼aLaughlin, Alexander Lewis.▼0(orcid)0000-0002-8605-5381
■24513▼aAn Investigation Into Copper Proteins Germane to Biological Ammonia Oxidation
■260 ▼a[Sl]▼bCornell University▼c2025
■260 1▼aAnn Arbor▼bProQuest Dissertations & Theses▼c2025
■300 ▼a122 p
■500 ▼aSource: Dissertations Abstracts International, Volume: 86-12, Section: B.
■500 ▼aAdvisor: Lancaster, Kyle.
■5021 ▼aThesis (Ph.D.)--Cornell University, 2025.
■520 ▼aIn lieu of carbon-based primary metabolisms found in plants and animals, certain bacteria and archaea survive by catabolizing ammonia. These organisms are globally pervasive and control biogeochemical nitrogen cycle fluxes. A dearth of understanding persists regarding the underlying biochemistry of these nitrogen-based metabolisms due to the difficulties associated with culturing ammonia-oxidizing organisms. Nevertheless, copper is known to play a vital role in biological ammonia oxidation (BAO).This thesis explores the biochemistry of two of the most abundant copper proteins in the model ammonia-oxidizing bacterium, Nitrosomonas europaea. Molecular biology and structural biology techniques are employed to develop a heterologous technology for the isolation of an integral membrane protein complex, which is believed to catalyze the first step of BAO, ammonia monooxygenase (AMO). Additionally, an investigation into the in vivo function of nitrosocyanin (Ncya) is made. Spectroscopic techniques are utilized to assess the activity and electron transfer kinetics of Ncya. The results provide insight into Ncya function and challenge proposed hypotheses.
■590 ▼aSchool code: 0058.
■650 4▼aChemistry
■650 4▼aMicrobiology
■650 4▼aBiochemistry
■653 ▼aBiological ammonia oxidation
■653 ▼aAmmonia monooxygenase
■653 ▼aNitrosocyanin
■653 ▼aNitrosomonas europaea
■690 ▼a0485
■690 ▼a0487
■690 ▼a0410
■71020▼aCornell University▼bChemistry and Chemical Biology.
■7730 ▼tDissertations Abstracts International▼g86-12B.
■790 ▼a0058
■791 ▼aPh.D.
■792 ▼a2025
■793 ▼aEnglish
■85640▼uhttp://www.riss.kr/pdu/ddodLink.do?id=T17356572▼nKERIS▼z이 자료의 원문은 한국교육학술정보원에서 제공합니다.
