Structure and function of atypically coordinated enzymatic mononuclear non-heme-Fe(II) centers
Mononuclear, non-heme-Fe(II) centers are key structures in O2 metabolism and catalyze an impressive variety of enzymatic reactions. While most are bound via two histidines and a carboxylate, some show a different organization. A short overview of atypically coordinated O2 dependent mononuclear-non-h...
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| Format: | Online |
| Language: | English |
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Elsevier Sequoia
2013
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4019311/ |
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pubmed-4019311 |
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pubmed-40193112014-05-19 Structure and function of atypically coordinated enzymatic mononuclear non-heme-Fe(II) centers Buongiorno, Daniela Straganz, Grit D. Review Mononuclear, non-heme-Fe(II) centers are key structures in O2 metabolism and catalyze an impressive variety of enzymatic reactions. While most are bound via two histidines and a carboxylate, some show a different organization. A short overview of atypically coordinated O2 dependent mononuclear-non-heme-Fe(II) centers is presented here Enzymes with 2-His, 3-His, 3-His-carboxylate and 4-His bound Fe(II) centers are discussed with a focus on their reactivity, metal ion promiscuity and recent progress in the elucidation of their enzymatic mechanisms. Observations concerning these and classically coordinated Fe(II) centers are used to understand the impact of the metal binding motif on catalysis. Elsevier Sequoia 2013-01-15 /pmc/articles/PMC4019311/ /pubmed/24850951 http://dx.doi.org/10.1016/j.ccr.2012.04.028 Text en © 2013 Elsevier B.V. https://creativecommons.org/licenses/by/4.0/ Open Access under CC BY 4.0 (https://creativecommons.org/licenses/by/4.0/) license |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
Buongiorno, Daniela Straganz, Grit D. |
| spellingShingle |
Buongiorno, Daniela Straganz, Grit D. Structure and function of atypically coordinated enzymatic mononuclear non-heme-Fe(II) centers |
| author_facet |
Buongiorno, Daniela Straganz, Grit D. |
| author_sort |
Buongiorno, Daniela |
| title |
Structure and function of atypically coordinated enzymatic mononuclear non-heme-Fe(II) centers |
| title_short |
Structure and function of atypically coordinated enzymatic mononuclear non-heme-Fe(II) centers |
| title_full |
Structure and function of atypically coordinated enzymatic mononuclear non-heme-Fe(II) centers |
| title_fullStr |
Structure and function of atypically coordinated enzymatic mononuclear non-heme-Fe(II) centers |
| title_full_unstemmed |
Structure and function of atypically coordinated enzymatic mononuclear non-heme-Fe(II) centers |
| title_sort |
structure and function of atypically coordinated enzymatic mononuclear non-heme-fe(ii) centers |
| description |
Mononuclear, non-heme-Fe(II) centers are key structures in O2 metabolism and catalyze an impressive variety of enzymatic reactions. While most are bound via two histidines and a carboxylate, some show a different organization. A short overview of atypically coordinated O2 dependent mononuclear-non-heme-Fe(II) centers is presented here Enzymes with 2-His, 3-His, 3-His-carboxylate and 4-His bound Fe(II) centers are discussed with a focus on their reactivity, metal ion promiscuity and recent progress in the elucidation of their enzymatic mechanisms. Observations concerning these and classically coordinated Fe(II) centers are used to understand the impact of the metal binding motif on catalysis. |
| publisher |
Elsevier Sequoia |
| publishDate |
2013 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4019311/ |
| _version_ |
1612088399121874944 |