The Resource Metal Sites in Proteins and Models : Iron Centres, edited by H.A.O. Hill, P.J. Sadler, A.J. Thomson, (electronic resource)

Metal Sites in Proteins and Models : Iron Centres, edited by H.A.O. Hill, P.J. Sadler, A.J. Thomson, (electronic resource)

Label
Metal Sites in Proteins and Models : Iron Centres
Title
Metal Sites in Proteins and Models
Title remainder
Iron Centres
Statement of responsibility
edited by H.A.O. Hill, P.J. Sadler, A.J. Thomson
Contributor
Editor
Editor
Subject
Language
  • eng
  • eng
Summary
Biological chemistry is a major frontier of inorganic chemistry. Three special volumes devoted to Metal Sites in Proteins and Models address the questions: how unusual ("entatic") are metal sites in metalloproteins and metalloenzymes compared to those in small coordination complexes? And if they are special, how do polypeptide chains and co-factors control this? The chapters deal with iron, with metal centres acting as Lewis acids, metals in phosphate enzymes, with vanadium, and with the wide variety of transition metal ions which act as redox centres. They illustrate in particular how the combined armoury of genetics and structure determination at the molecular level are providing unprecedented new tools for molecular engineering
Member of
Dewey number
  • 541.2/2 s
  • 572/.7517
http://bibfra.me/vocab/relation/httpidlocgovvocabularyrelatorsedt
  • nvGTQqepgWE
  • HU3rH7fVMuE
  • yjaTUYqgklw
Image bit depth
0
Language note
English
LC call number
QD146-197
Literary form
non fiction
http://library.link/vocab/relatedWorkOrContributorName
  • Hill, H.A.O.
  • Sadler, P.J.
  • Thomson, A.J.
Series statement
Springer Desktop Editions in Chemistry
http://library.link/vocab/subjectName
  • Chemistry, inorganic
  • Biochemistry
  • Medicine
  • Cytology
  • Inorganic Chemistry
  • Biochemistry, general
  • Molecular Medicine
  • Cell Biology
  • Biological and Medical Physics, Biophysics
Label
Metal Sites in Proteins and Models : Iron Centres, edited by H.A.O. Hill, P.J. Sadler, A.J. Thomson, (electronic resource)
Instantiates
Publication
Note
Bibliographic Level Mode of Issuance: Monograph
Antecedent source
mixed
Carrier category
online resource
Carrier category code
  • cr
Color
not applicable
Content category
text
Content type code
  • txt
Contents
Polyiron oxides, oxyhydroxides and hydroxides as models for biomineralisation processes -- Heme: The most versatile redox centre in biology? -- Rationalisation of metal binding to transferrin: Prediction of metal-protein stability constants -- Metal centres of bacterioferritins or non-haem-iron-containing cytochromes b 557 -- Ribonucleotide reductases — a group of enzymes with different metallosites and a similar reaction mechanism -- Protein engineering of cytochrome P450cam
Dimensions
unknown
Edition
1st ed. 1997.
Extent
1 online resource (VII, 207 p.)
File format
multiple file formats
Form of item
online
Isbn
9783540690351
Level of compression
uncompressed
Media category
computer
Media type code
  • c
Other control number
10.1007/3-540-62870-3
Quality assurance targets
absent
Reformatting quality
access
Specific material designation
remote
System control number
  • (CKB)1000000000234631
  • (SSID)ssj0000324778
  • (PQKBManifestationID)11242149
  • (PQKBTitleCode)TC0000324778
  • (PQKBWorkID)10314889
  • (PQKB)10734556
  • (DE-He213)978-3-540-69035-1
  • (EXLCZ)991000000000234631
Label
Metal Sites in Proteins and Models : Iron Centres, edited by H.A.O. Hill, P.J. Sadler, A.J. Thomson, (electronic resource)
Publication
Note
Bibliographic Level Mode of Issuance: Monograph
Antecedent source
mixed
Carrier category
online resource
Carrier category code
  • cr
Color
not applicable
Content category
text
Content type code
  • txt
Contents
Polyiron oxides, oxyhydroxides and hydroxides as models for biomineralisation processes -- Heme: The most versatile redox centre in biology? -- Rationalisation of metal binding to transferrin: Prediction of metal-protein stability constants -- Metal centres of bacterioferritins or non-haem-iron-containing cytochromes b 557 -- Ribonucleotide reductases — a group of enzymes with different metallosites and a similar reaction mechanism -- Protein engineering of cytochrome P450cam
Dimensions
unknown
Edition
1st ed. 1997.
Extent
1 online resource (VII, 207 p.)
File format
multiple file formats
Form of item
online
Isbn
9783540690351
Level of compression
uncompressed
Media category
computer
Media type code
  • c
Other control number
10.1007/3-540-62870-3
Quality assurance targets
absent
Reformatting quality
access
Specific material designation
remote
System control number
  • (CKB)1000000000234631
  • (SSID)ssj0000324778
  • (PQKBManifestationID)11242149
  • (PQKBTitleCode)TC0000324778
  • (PQKBWorkID)10314889
  • (PQKB)10734556
  • (DE-He213)978-3-540-69035-1
  • (EXLCZ)991000000000234631

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