메뉴 건너뛰기




Volumn 314, Issue 3, 2004, Pages 793-797

PQQ glucose dehydrogenase with novel electron transfer ability

Author keywords

Cytochrome; Direct electron transfer type sensor; Electron transfer; Glucose sensor; PQQ glucose dehydrogenase

Indexed keywords

ALCOHOL DEHYDROGENASE; ALCOHOL DEHYDROGENASE (ACCEPTOR); CYTOCHROME C; GLUCOSE; GLUCOSE DEHYDROGENASE; GLUCOSE DEHYDROGENASE (PYRROLOQUINOLINE QUINONE); GLUCOSE DEHYDROGENASE (PYRROLOQUINOLINE-QUINONE); HYBRID PROTEIN;

EID: 1642578975     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2003.12.167     Document Type: Article
Times cited : (54)

References (21)
  • 1
    • 0029643953 scopus 로고
    • The refined structure of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens at 1.94 angstrom
    • Ghosh M., Anthony C., Harlos K., Goodwin M.G., Blake C. The refined structure of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens at 1.94 angstrom. Structure. 3:1995;177-187.
    • (1995) Structure , vol.3 , pp. 177-187
    • Ghosh, M.1    Anthony, C.2    Harlos, K.3    Goodwin, M.G.4    Blake, C.5
  • 2
    • 0025188604 scopus 로고
    • Cloning, mapping, and sequencing of the gene encoding Escherichia coli quinoprotein glucose dehydrogenase
    • Cleton-jansen A.M., Goosen N., Fayet O., Vandeputte P. Cloning, mapping, and sequencing of the gene encoding Escherichia coli quinoprotein glucose dehydrogenase. J. Bacteriol. 172:1990;6308-6315.
    • (1990) J. Bacteriol. , vol.172 , pp. 6308-6315
    • Cleton-Jansen, A.M.1    Goosen, N.2    Fayet, O.3    Vandeputte, P.4
  • 3
    • 0038312036 scopus 로고    scopus 로고
    • Escherichia coli PQQ-containing quinoprotein glucose dehydrogenase: Its structure comparison with other quinoproteins
    • Yamada M., Elias M.D., Matsushita K., Migita C.T., Adachi O. Escherichia coli PQQ-containing quinoprotein glucose dehydrogenase: its structure comparison with other quinoproteins. BBA-Proteins Proteomics. 1647:2003;185-192.
    • (2003) BBA-Proteins Proteomics , vol.1647 , pp. 185-192
    • Yamada, M.1    Elias, M.D.2    Matsushita, K.3    Migita, C.T.4    Adachi, O.5
  • 4
    • 0028584412 scopus 로고
    • The structure and function of methanol dehydrogenase and related quinoproteins containing pyrrolo-quinoline quinone
    • Anthony C., Ghosh M., Blake C.C.F. The structure and function of methanol dehydrogenase and related quinoproteins containing pyrrolo-quinoline quinone. Biochem. J. 304:1994;665-674.
    • (1994) Biochem. J. , vol.304 , pp. 665-674
    • Anthony, C.1    Ghosh, M.2    Blake, C.C.F.3
  • 5
    • 0021525297 scopus 로고
    • Quinoprotein alcohol dehydrogenase from ethanol-grown Pseudomonas aeruginosa
    • Groen B., Frank J. Jr., Duine J.A. Quinoprotein alcohol dehydrogenase from ethanol-grown Pseudomonas aeruginosa. Biochem. J. 223:1984;921-924.
    • (1984) Biochem. J. , vol.223 , pp. 921-924
    • Groen, B.1    Frank, J.Jr.2    Duine, J.A.3
  • 6
    • 0036479218 scopus 로고    scopus 로고
    • Crystal structure of quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni - Structural basis for substrate oxidation and electron transfer
    • Oubrie A., Rozeboom H.J., Kalk K.H., Huizinga E.G., Dijkstra B.W. Crystal structure of quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni - structural basis for substrate oxidation and electron transfer. J. Biol. Chem. 277:2002;3727-3732.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3727-3732
    • Oubrie, A.1    Rozeboom, H.J.2    Kalk, K.H.3    Huizinga, E.G.4    Dijkstra, B.W.5
  • 7
    • 0036162632 scopus 로고    scopus 로고
    • Direct bioelectrocatalysis at carbon electrodes modified with quinohemoprotein alcohol dehydrogenase from Gluconobacter sp. 33
    • Razumiene J., Niculescu M., Ramanavicius A., Laurinavicius V., Csoregi E. Direct bioelectrocatalysis at carbon electrodes modified with quinohemoprotein alcohol dehydrogenase from Gluconobacter sp. 33. Electroanalysis. 14:2002;43-49.
    • (2002) Electroanalysis , vol.14 , pp. 43-49
    • Razumiene, J.1    Niculescu, M.2    Ramanavicius, A.3    Laurinavicius, V.4    Csoregi, E.5
  • 8
    • 0000933312 scopus 로고
    • Bioelectrocatalysis at electrodes coated with alcohol dehydrogenase, a quinohemoprotein with heme c serving as a built-in mediator
    • Ikeda T., Kobayashi D., Matsushita F., Sagara T., Niki K. Bioelectrocatalysis at electrodes coated with alcohol dehydrogenase, a quinohemoprotein with heme c serving as a built-in mediator. J. Electroanal. Chem. 361:1993;221-228.
    • (1993) J. Electroanal. Chem. , vol.361 , pp. 221-228
    • Ikeda, T.1    Kobayashi, D.2    Matsushita, F.3    Sagara, T.4    Niki, K.5
  • 9
    • 0000262327 scopus 로고
    • Enzyme-catalyzed electrochemical oxidation of D-gluconate at electrodes coated with D-gluconate dehydrogenase, a membrane-bound flavohemoprotein
    • Ikeda T., Miyaoka S., Miki K. Enzyme-catalyzed electrochemical oxidation of D-gluconate at electrodes coated with D-gluconate dehydrogenase, a membrane-bound flavohemoprotein. J. Electroanal. Chem. 352:1993;267-278.
    • (1993) J. Electroanal. Chem. , vol.352 , pp. 267-278
    • Ikeda, T.1    Miyaoka, S.2    Miki, K.3
  • 10
    • 0032742692 scopus 로고    scopus 로고
    • Active-site structure of the soluble quinoprotein glucose dehydrogenase complexed with methylhydrazine: A covalent cofactor-inhibitor complex
    • Oubrie A., Rozeboom H.J., Dijkstra B.W. Active-site structure of the soluble quinoprotein glucose dehydrogenase complexed with methylhydrazine: A covalent cofactor-inhibitor complex. Proc. Natl. Acad. Sci. USA. 96:1999;11787-11791.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11787-11791
    • Oubrie, A.1    Rozeboom, H.J.2    Dijkstra, B.W.3
  • 11
    • 0034524811 scopus 로고    scopus 로고
    • The role of conserved His775/781 in membrane-binding PQQ glucose dehyrogenase of Escherichia coli and Acinetobacter calcoacericus
    • Okuda J., Yoshida H., Kojima K., Sode K. The role of conserved His775/ 781 in membrane-binding PQQ glucose dehyrogenase of Escherichia coli and Acinetobacter calcoacericus. J. Biochem. Mol. Biol. Biophys. 4:2000;415-422.
    • (2000) J. Biochem. Mol. Biol. Biophys. , vol.4 , pp. 415-422
    • Okuda, J.1    Yoshida, H.2    Kojima, K.3    Sode, K.4
  • 12
    • 0028587627 scopus 로고
    • Over expression of PQQ glucose dehydrogenase in Escherichia coli under holo enzyme forming condition
    • Sode K., Witarto A.B., Watanabe K., Noda K., Ito S., Tsugawa W. Over expression of PQQ glucose dehydrogenase in Escherichia coli under holo enzyme forming condition. Biotechnol. Lett. 16:1994;1265-1268.
    • (1994) Biotechnol. Lett. , vol.16 , pp. 1265-1268
    • Sode, K.1    Witarto, A.B.2    Watanabe, K.3    Noda, K.4    Ito, S.5    Tsugawa, W.6
  • 13
    • 0034079533 scopus 로고    scopus 로고
    • Increasing the thermal stability of the water-soluble pyrroloquinoline quinone glucose dehydrogenase by single amino acid replacement
    • Sode K., Ootera T., Shirahane M., Witarto A.B., Igarashi S., Yoshida H. Increasing the thermal stability of the water-soluble pyrroloquinoline quinone glucose dehydrogenase by single amino acid replacement. Enzyme Microb. Technol. 26:2000;491-496.
    • (2000) Enzyme Microb. Technol. , vol.26 , pp. 491-496
    • Sode, K.1    Ootera, T.2    Shirahane, M.3    Witarto, A.B.4    Igarashi, S.5    Yoshida, H.6
  • 14
    • 0032578852 scopus 로고    scopus 로고
    • Overproduction of the Bradyrhizobium japonicum c-type cytochrome subunits of the cbb(3) oxidase in Escherichia coli
    • Arslan E., Schulz H., Zufferey R., Kunzler P., Thony-Meyer L. Overproduction of the Bradyrhizobium japonicum c-type cytochrome subunits of the cbb(3) oxidase in Escherichia coli. Biochem. Biophys. Res. Commun. 251:1998;744-747.
    • (1998) Biochem. Biophys. Res. Commun. , vol.251 , pp. 744-747
    • Arslan, E.1    Schulz, H.2    Zufferey, R.3    Kunzler, P.4    Thony-Meyer, L.5
  • 15
    • 0028587627 scopus 로고
    • Over expression of PQQ glucose dehydrogenase in Escherichia coli under holo enzyme forming condition
    • Sode K., Witarto A.B., Watanabe K., Noda K., Ito S., Tsugawa W. Over expression of PQQ glucose dehydrogenase in Escherichia coli under holo enzyme forming condition. Biotechnol. Lett. 16:1994;1265-1268.
    • (1994) Biotechnol. Lett. , vol.16 , pp. 1265-1268
    • Sode, K.1    Witarto, A.B.2    Watanabe, K.3    Noda, K.4    Ito, S.5    Tsugawa, W.6
  • 16
    • 0036901886 scopus 로고    scopus 로고
    • Construction of engineered water-soluble PQQ glucose dehydrogenase with improved substrate specificity
    • Sode K., Igarashi S., Morimoto A., Yoshida H. Construction of engineered water-soluble PQQ glucose dehydrogenase with improved substrate specificity. Biocatal. Biotransform. 20:2002;405-412.
    • (2002) Biocatal. Biotransform. , vol.20 , pp. 405-412
    • Sode, K.1    Igarashi, S.2    Morimoto, A.3    Yoshida, H.4
  • 18
    • 0037403199 scopus 로고    scopus 로고
    • Glucose enzyme electrode using cytochrome b(562) as an electron mediator
    • Okuda J., Wakai J., Yuhashi N., Sode K. Glucose enzyme electrode using cytochrome b(562) as an electron mediator. Biosens. Bioelectron. 18:2003;699-704.
    • (2003) Biosens. Bioelectron. , vol.18 , pp. 699-704
    • Okuda, J.1    Wakai, J.2    Yuhashi, N.3    Sode, K.4
  • 19
    • 0028855015 scopus 로고
    • Soluble and membrane-bound quinoprotein D-glucose dehydrogenases of the Acinetobacter calcoaceticus - The binding process of PQQ to the apoenzymes
    • Matsushita K., Toyama H., Ameyama M., Adachi O., Dewanti A., Duine J.A. Soluble and membrane-bound quinoprotein D-glucose dehydrogenases of the Acinetobacter calcoaceticus - the binding process of PQQ to the apoenzymes. Biosci. Biotechnol. Biochem. 59:1995;1548-1555.
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 1548-1555
    • Matsushita, K.1    Toyama, H.2    Ameyama, M.3    Adachi, O.4    Dewanti, A.5    Duine, J.A.6
  • 20
    • 0036368346 scopus 로고    scopus 로고
    • The application of cytochromes as the interface molecule to facilitate the electron transfer for PQQ glucose dehydrogenase employing mediator type glucose sensor
    • Okuda J., Wakai J., Sode K. The application of cytochromes as the interface molecule to facilitate the electron transfer for PQQ glucose dehydrogenase employing mediator type glucose sensor. Anal. Lett. 35:2002;1465-1478.
    • (2002) Anal. Lett. , vol.35 , pp. 1465-1478
    • Okuda, J.1    Wakai, J.2    Sode, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.