$\require{mediawiki-texvc}$

연합인증

연합인증 가입 기관의 연구자들은 소속기관의 인증정보(ID와 암호)를 이용해 다른 대학, 연구기관, 서비스 공급자의 다양한 온라인 자원과 연구 데이터를 이용할 수 있습니다.

이는 여행자가 자국에서 발행 받은 여권으로 세계 각국을 자유롭게 여행할 수 있는 것과 같습니다.

연합인증으로 이용이 가능한 서비스는 NTIS, DataON, Edison, Kafe, Webinar 등이 있습니다.

한번의 인증절차만으로 연합인증 가입 서비스에 추가 로그인 없이 이용이 가능합니다.

다만, 연합인증을 위해서는 최초 1회만 인증 절차가 필요합니다. (회원이 아닐 경우 회원 가입이 필요합니다.)

연합인증 절차는 다음과 같습니다.

최초이용시에는
ScienceON에 로그인 → 연합인증 서비스 접속 → 로그인 (본인 확인 또는 회원가입) → 서비스 이용

그 이후에는
ScienceON 로그인 → 연합인증 서비스 접속 → 서비스 이용

연합인증을 활용하시면 KISTI가 제공하는 다양한 서비스를 편리하게 이용하실 수 있습니다.

Structural Basis for the Changes in Redox Potential in the Nitrogenase Phe135Trp Fe Protein with MgADP Bound 원문보기

Molecules and cells, v.18 no.3, 2004년, pp.374 - 382  

Jeong, Mi Suk ,  Jang, Se Bok

Abstract AI-Helper 아이콘AI-Helper

The crystal structure of the Azotobacter vinelandii nitrogenase Fe protein with phenylalanine at position 135 substituted by tryptophan has been determined in MgADP-bound form by X-ray diffraction methods. Amino acid substitution studies have suggested that the phenylalanine at position 135 located ...

참고문헌 (42)

  1. Acta Crystallogr. D Biol. Crystallogr. Abrahams 52 30 1996 10.1107/S0907444995008754 Methods used in the structure determination of bovine mitochondrial F(1) ATPase. 

  2. Proc. Natl. Acad. Sci. USA Adman 72 4854 1975 10.1073/pnas.72.12.4854 NH---S hydrogen bonds in Peptococcus aerogenes ferredoxin, Clostridium pasteurianum rubredoxin, and Chromatium high potential iron protein. 

  3. J. Am. Chem. Soc. Backes 113 2055 1991 10.1021/ja00006a027 The environment of Fe4S4 clusters in ferredoxins and high-potential iron proteins. New information from X-ray crystallography and resonance Raman spectroscopy. 

  4. J. Biol. Chem. Breiter 266 18660 1991 10.1016/S0021-9258(18)55114-0 The molecular structure of the high potential ironsulfur protein isolated from Ectothiorhodospira halophila determined at 2.5-A resolution. 

  5. Nature Brunger 355 472 1992 10.1038/355472a0 The free R value: a novel statistical quantity for assessing the accuracy of crystal structures. 

  6. Brunger 1992 X-PLOR version 3.1 - A system for X-ray crystallography and NMR 

  7. Science Brunger 235 458 1987 10.1126/science.235.4787.458 Crystallographic R factor refinement by molecular dynamics. 

  8. Burgess 103 1984 in advances in nitrogen fixation 

  9. Chem. Rev. Burgess 96 2983 1996 10.1021/cr950055x Mechanism of molybdenum nitrogenase. 

  10. J. Biol. Chem. Burris 266 9339 1991 10.1016/S0021-9258(18)92821-8 Nitrogenases. 

  11. J. Biol. Chem. Carter 252 7802 1977 10.1016/S0021-9258(17)41038-6 New stereochemical analogies between iron-sulfur electron transport proteins. 

  12. Clin. Chem. Chromy 20 1362 1974 10.1093/clinchem/20.10.1362 Re-evaluation of EDTA-chelated biuret reagent. 

  13. Biochemistry Churg 25 1675 1986 10.1021/bi00355a035 Control of the redox potential of cytochrome c and microscopic dielectric effects in proteins. 

  14. Acta Crystallogr. D Biol. Crystallogr. Cowtain 49 148 1993 10.1107/S0907444992007698 Improvement of macromolecular electron-density maps by the simultaneous application of real and reciprocal space constraints. 

  15. Science Georgiadis 257 1653 1992 10.1126/science.1529353 Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii. 

  16. Methods Enzymol. Hathaway 60 495 1979 10.1016/S0076-6879(79)60047-2 Isolation of protein kinases from reticulocytes and phosphorylation of initiation factors. 

  17. Annu. Rev. Biochem. Howard 63 235 1994 10.1146/annurev.bi.63.070194.001315 Nitrogenase: a nucleotidedependent molecular switch. 

  18. Protein Sci. Iwagami 4 2562 1995 10.1002/pro.5560041213 The role of a conserved tyrosine residue in high-potential iron sulfur proteins. 

  19. Biochemistry Jang 39 641 2000 10.1021/bi991694v Modulating the midpoint potential of the [4Fe-4S] cluster of the nitrogenase Fe protein. 

  20. Biochemistry Jang 39 14745 2000 10.1021/bi001705g Insights into nucleotide signal transduction in nitrogenase: structure of an iron protein with MgADP bound. 

  21. Biochemistry Jensen 33 10911 1994 10.1021/bi00202a010 Calculation of the redox potentials of iron-sulfur proteins: the 2-/3-couple of [Fe4S*4Cys4] clusters in Peptococcus aerogenes ferredoxin, Azotobacter vinelandii ferredoxin I, and Chromatium vinosum high-potential iron protein. 

  22. Acta Crystallogr. A Jones 47 110 1991 10.1107/S0108767390010224 Improved methods for building protein models in electron density maps and the location of errors in these models. 

  23. Science Kim 257 1677 1992 10.1126/science.1529354 Structural models for the metal centers in the nitrogenase molybdenum-iron protein. 

  24. J. Biol. Chem. Langen 267 25625 1992 10.1016/S0021-9258(18)35647-3 Protein control of iron-sulfur cluster redox potentials. 

  25. Biochemistry Lanzilotta 34 10713 1995 10.1021/bi00034a003 Nucleotide hydrolysis and protein conformational changes in Azotobacter vinelandii nitrogenase iron protein: defining the function of aspartate 129. 

  26. Biochemistry Ljones 17 1866 1978 10.1021/bi00603a010 Nitrogenase: the reaction between the Fe protein and bathophenanthrolinedisulfonate as a probe for interactions with MgATP. 

  27. Adv. Enzymol. Rel. Areas Mol. Biol. Mortenson 67 299 1993 The role of metal-clusters and MgATP in nitrogenase catalysis. 

  28. Acta Crystallogr. D Biol. Crystallogr. Navaza 50 1507 1994 On the computation of the fast rotation function. 

  29. Acc. Chem. Res. Ortiz-Johnson 20 289 1987 10.1021/ar00140a004 Control of the catalytic activity of prosthetic heme by the structure of hemoproteins. 

  30. Otwinowski, Z. (1993) in Data Collection and Processing, SERC Daresbury Laboratory, Daresbury, pp. 56-62, U. K. 

  31. Annu. Rev. Microbiol. Peters 49 335 1995 10.1146/annurev.mi.49.100195.002003 Nitrogenase structure and function: A biochemical-genetic perspective. 

  32. Biochemistry Ryle 35 4766 1996 10.1021/bi960026w Elucidation of a MgATP signal transduction pathway in the nitrogenase iron protein: formation of a conformation resembling the MgATP-bound state by protein engineering. 

  33. J. Biol. Chem. Ryle 270 13112 1995 10.1074/jbc.270.22.13112 Evidence for a central role of lysine 15 of Azotobacter vinelandii nitrogenase iron protein in nucleotide binding and protein conformational changes. 

  34. Nature Schindelin 387 370 1997 10.1038/387370a0 Structure of ADP × AIF4(-)-stabilized nitrogenase complex and its implications for signal transduction. 

  35. J. Mol. Biol. Schlessman 280 669 1998 10.1006/jmbi.1998.1898 Conformational variability in structures of the nitrogenase iron proteins from Azotobacter vinelandii and Clostridium pasteurianum. 

  36. Protein Sci. Seefeldt 2 93 1993 10.1002/pro.5560020110 Increasing nitrogenase catalytic efficiency for MgATP by changing serine 16 of its Fe protein to threonine: use of Mn2+to show interaction of serine 16 with Mg2+. 

  37. Science Simpson 224 1095 1984 10.1126/science.6585956 A nitrogen pressure of 50 atmospheres does not prevent evolution of hydrogen by nitrogenase. 

  38. Eur. J. Biochem. Smith 205 1 1992 10.1111/j.1432-1033.1992.tb16746.x Metalloclusters of the nitrogenases. 

  39. Chem. Rev. Stephens 96 2491 1996 10.1021/cr950045w Protein control of redox potentials of ironminus sign sulfur proteins. 

  40. Biochemistry Vidakovic 34 13906 1995 10.1021/bi00042a023 The environment of [2Fe-2S] clusters in ferredoxins: the role of residue 45 probed by site-directed mutagenesis. 

  41. Mol. Cells Yoon 16 266 2003 10.1016/S1016-8478(23)13799-X X-ray crystallographic studies of HemK from Thermotoga maritima, an N5-glutamine methyltransferase. 

  42. Biochemistry Yu 34 7861 1995 10.1021/bi00024a010 Evidence for a mixed-ligand [4Fe-4S] cluster in the C14D mutant of PsaC. Altered reduction potentials and EPR spectral properties of the FA and FB clusters on rebinding to the P700-FX core. 

관련 콘텐츠

원문 보기

원문 URL 링크

*원문 PDF 파일 및 링크정보가 존재하지 않을 경우 KISTI DDS 시스템에서 제공하는 원문복사서비스를 사용할 수 있습니다.

오픈액세스(OA) 유형

BRONZE

출판사/학술단체 등이 한시적으로 특별한 프로모션 또는 일정기간 경과 후 접근을 허용하여, 출판사/학술단체 등의 사이트에서 이용 가능한 논문

섹션별 컨텐츠 바로가기

AI-Helper ※ AI-Helper는 오픈소스 모델을 사용합니다.

AI-Helper 아이콘
AI-Helper
안녕하세요, AI-Helper입니다. 좌측 "선택된 텍스트"에서 텍스트를 선택하여 요약, 번역, 용어설명을 실행하세요.
※ AI-Helper는 부적절한 답변을 할 수 있습니다.

선택된 텍스트

맨위로