WO2007090873A3 - Oxidoreductases and processes utilising such enzymes - Google Patents

Oxidoreductases and processes utilising such enzymes Download PDF

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Publication number
WO2007090873A3
WO2007090873A3 PCT/EP2007/051232 EP2007051232W WO2007090873A3 WO 2007090873 A3 WO2007090873 A3 WO 2007090873A3 EP 2007051232 W EP2007051232 W EP 2007051232W WO 2007090873 A3 WO2007090873 A3 WO 2007090873A3
Authority
WO
WIPO (PCT)
Prior art keywords
kcat
site
type
nitrite reductase
catalytic activity
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Ceased
Application number
PCT/EP2007/051232
Other languages
French (fr)
Other versions
WO2007090873A2 (en
WO2007090873B1 (en
Inventor
Gerard W Canters
Hein Jakob Wijma
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Universiteit Leiden
Original Assignee
Universiteit Leiden
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Universiteit Leiden filed Critical Universiteit Leiden
Priority to US12/223,850 priority Critical patent/US20100167311A1/en
Priority to EP07712192A priority patent/EP1987154A2/en
Priority to AU2007213656A priority patent/AU2007213656A1/en
Priority to CA002638890A priority patent/CA2638890A1/en
Publication of WO2007090873A2 publication Critical patent/WO2007090873A2/en
Publication of WO2007090873A3 publication Critical patent/WO2007090873A3/en
Publication of WO2007090873B1 publication Critical patent/WO2007090873B1/en
Anticipated expiration legal-status Critical
Ceased legal-status Critical Current

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Classifications

    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
    • C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
    • C12Q1/001—Enzyme electrodes
    • C12Q1/005—Enzyme electrodes involving specific analytes or enzymes

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  • Chemical & Material Sciences (AREA)
  • Organic Chemistry (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Health & Medical Sciences (AREA)
  • Wood Science & Technology (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Zoology (AREA)
  • Engineering & Computer Science (AREA)
  • Immunology (AREA)
  • General Engineering & Computer Science (AREA)
  • Microbiology (AREA)
  • Molecular Biology (AREA)
  • Analytical Chemistry (AREA)
  • Biotechnology (AREA)
  • Physics & Mathematics (AREA)
  • Biochemistry (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Biophysics (AREA)
  • General Health & Medical Sciences (AREA)
  • Genetics & Genomics (AREA)
  • Enzymes And Modification Thereof (AREA)
  • Micro-Organisms Or Cultivation Processes Thereof (AREA)
  • Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
  • Investigating Or Analysing Biological Materials (AREA)
  • Peptides Or Proteins (AREA)

Abstract

In Cu-containing nitrite reductase from Alcaligenes faecalis S-6 the axial methionine ligand of the type1 site was replaced (M150G) to make the copper atom accessible to external ligands that might affect the enzyme's catalytic activity. The type-1 site optical spectrum of M150G (A460/A600 = 0.71) differs significantly from that of the native nitrite reductase (A460/A600 = 1.3). The reduction potential of the type-1 site of nitrite reductase M150G (EM = 312 - 5 mV versus hydrogen) is higher than that of the native enzyme (EM = 213 - 5 mV). M150G has a lower catalytic activity (kcat = 133 - 6 s-1) than the wild-type nitrite reductase (kcat = 416 - 10 - s 1). The binding of external ligands to M150G restores spectral properties, reduction potential (EM < 225 mV), and catalytic activity (kcat = 374 - 28 s-1). Also the M150H (A460/A600 = 7.7, EM = 104 - 5 mV, kcat = 0.099 - 0.006 s-1) and M150T (A460/A600 = 0.085, EM = 340 - 5 mV, kcat = 126 - 2 s -1) variants were characterized to compare their properties with those of M150G. Crystal structures show that the ligands act as allosteric effectors by displacing Met62 which moves to bind to the Cu in the position emptied by the M150G mutation. The reconstituted type-1 site has an otherwise unaltered geometry. The observation that a rearranged ligand can introduce allosteric control in a redox enzyme suggests potential for structural and functional flexibility of copper-containing redox sites.
PCT/EP2007/051232 2006-02-09 2007-02-08 Oxidoreductases and processes utilising such enzymes Ceased WO2007090873A2 (en)

Priority Applications (4)

Application Number Priority Date Filing Date Title
US12/223,850 US20100167311A1 (en) 2006-02-09 2007-02-08 Oxidoreductases and Processes Utilising Such Enzymes
EP07712192A EP1987154A2 (en) 2006-02-09 2007-02-08 Oxidoreductases and processes utilising such enzymes
AU2007213656A AU2007213656A1 (en) 2006-02-09 2007-02-08 Oxidoreductases and processes utilising such enzymes
CA002638890A CA2638890A1 (en) 2006-02-09 2007-02-08 Oxidoreductases and processes utilising such enzymes

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
EP06250703.3 2006-02-09
EP06250703 2006-02-09

Publications (3)

Publication Number Publication Date
WO2007090873A2 WO2007090873A2 (en) 2007-08-16
WO2007090873A3 true WO2007090873A3 (en) 2007-10-04
WO2007090873B1 WO2007090873B1 (en) 2008-01-03

Family

ID=36441688

Family Applications (1)

Application Number Title Priority Date Filing Date
PCT/EP2007/051232 Ceased WO2007090873A2 (en) 2006-02-09 2007-02-08 Oxidoreductases and processes utilising such enzymes

Country Status (5)

Country Link
US (1) US20100167311A1 (en)
EP (1) EP1987154A2 (en)
AU (1) AU2007213656A1 (en)
CA (1) CA2638890A1 (en)
WO (1) WO2007090873A2 (en)

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN102495011B (en) * 2011-11-24 2013-08-14 上海应用技术学院 Method for determining activity of bacterial nitrite reductase

Families Citing this family (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2013012391A1 (en) * 2011-07-21 2013-01-24 National University Of Singapore A redox flow battery system
US10839149B2 (en) 2016-02-01 2020-11-17 Microsoft Technology Licensing, Llc. Generating templates from user's past documents
US9922022B2 (en) * 2016-02-01 2018-03-20 Microsoft Technology Licensing, Llc. Automatic template generation based on previous documents
CN114894871B (en) * 2022-05-16 2024-01-16 安徽大学 Preparation method and application of high-sensitivity nitrite reductase bioelectrode

Citations (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5403450A (en) * 1990-09-26 1995-04-04 Mobitec Molecular Biologische Technologie Gmbh Method of water purification

Patent Citations (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5403450A (en) * 1990-09-26 1995-04-04 Mobitec Molecular Biologische Technologie Gmbh Method of water purification

Non-Patent Citations (5)

* Cited by examiner, † Cited by third party
Title
ALBERS W M ET AL: "Design of novel molecular wires for realizing long-distance electron transfer", BIOELECTROCHEMISTRY AND BIOENERGETICS 1997 SWITZERLAND, vol. 42, no. 1, 1997, pages 25 - 33, XP002383492, ISSN: 0302-4598 *
ASTIER YANN ET AL: "Sensing nitrite through a pseudoazurin-nitrite reductase electron transfer relay.", CHEMPHYSCHEM : A EUROPEAN JOURNAL OF CHEMICAL PHYSICS AND PHYSICAL CHEMISTRY. 13 JUN 2005, vol. 6, no. 6, 13 June 2005 (2005-06-13), pages 1114 - 1120, XP002383493, ISSN: 1439-4235 *
SASAKI S ET AL: "Application of nitrite reductase from Alcaligenes faecalis S-6 for nitrite measurement.", BIOSENSORS & BIOELECTRONICS. 1 JAN 1998, vol. 13, no. 1, 1 January 1998 (1998-01-01), pages 1 - 5, XP002383494, ISSN: 0956-5663 *
VERBEET, M.PH., JEUKEN, L.J.C., WIJMA, H.J., FITTIPALDI, M., BOULANGER, M. J., HUBER, M., MURPHY,M.E.P., CANTERS, G.W.: "Engineering Type-1 Copper Centres in Redox Enzymes for Hot Wiring", BOOKLET OF THE NIGMS MEETING "METALS IN MEDICINE: TARGETS, DIAGNOSIS AND THERAPEUTICS", June 2000 (2000-06-01), Natcher Conference Center, Bethesda, USA, pages 79 - 80, XP002383491 *
WIJMA HEIN J ET AL: "Reconstitution of the type-1 active site of the H145G/A variants of nitrite reductase by ligand insertion.", BIOCHEMISTRY. 15 APR 2003, vol. 42, no. 14, 15 April 2003 (2003-04-15), pages 4075 - 4083, XP002383490, ISSN: 0006-2960 *

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN102495011B (en) * 2011-11-24 2013-08-14 上海应用技术学院 Method for determining activity of bacterial nitrite reductase

Also Published As

Publication number Publication date
EP1987154A2 (en) 2008-11-05
WO2007090873A2 (en) 2007-08-16
CA2638890A1 (en) 2007-08-16
AU2007213656A1 (en) 2007-08-16
US20100167311A1 (en) 2010-07-01
WO2007090873B1 (en) 2008-01-03

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