Dioxygen binding is controlled by the protein environment in non-heme FeII and 2-oxoglutarate oxygenases: a study on histone demethylase PHF8 and an ethylene-forming enzyme

Invited for the cover of this issue are Christo Z. Christov and co-workers at Michigan Technological University, University of Oxford, and Michigan State University. The image depicts the oxygen diffusion channel in class 7 histone demethylase (PHF8) and ethylene-forming enzyme (EFE) and changes in...

Full description

Bibliographic Details
Main Authors: Chaturvedi, SS, Thomas, MG, Bathir Jaber Sathik Rifayee, S, White, W, Wildey, J, Warner, C, Schofield, CJ, Hu, J, Hausinger, RP, Karabencheva-Christova, TG, Christov, CZ
Format: Journal article
Language:English
Published: Wiley 2023
_version_ 1797113112867897344
author Chaturvedi, SS
Thomas, MG
Bathir Jaber Sathik Rifayee, S
White, W
Wildey, J
Warner, C
Schofield, CJ
Hu, J
Hausinger, RP
Karabencheva-Christova, TG
Christov, CZ
author_facet Chaturvedi, SS
Thomas, MG
Bathir Jaber Sathik Rifayee, S
White, W
Wildey, J
Warner, C
Schofield, CJ
Hu, J
Hausinger, RP
Karabencheva-Christova, TG
Christov, CZ
author_sort Chaturvedi, SS
collection OXFORD
description Invited for the cover of this issue are Christo Z. Christov and co-workers at Michigan Technological University, University of Oxford, and Michigan State University. The image depicts the oxygen diffusion channel in class 7 histone demethylase (PHF8) and ethylene-forming enzyme (EFE) and changes in the enzymes’ conformations upon binding. Read the full text of the article at 10.1002/chem.202300138.
first_indexed 2024-03-07T08:01:43Z
format Journal article
id oxford-uuid:3216b6ae-c677-4414-b7cd-d083e85f74a6
institution University of Oxford
language English
last_indexed 2024-04-09T03:57:32Z
publishDate 2023
publisher Wiley
record_format dspace
spelling oxford-uuid:3216b6ae-c677-4414-b7cd-d083e85f74a62024-04-04T10:15:56ZDioxygen binding is controlled by the protein environment in non-heme FeII and 2-oxoglutarate oxygenases: a study on histone demethylase PHF8 and an ethylene-forming enzymeJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:3216b6ae-c677-4414-b7cd-d083e85f74a6EnglishSymplectic ElementsWiley2023Chaturvedi, SSThomas, MGBathir Jaber Sathik Rifayee, SWhite, WWildey, JWarner, CSchofield, CJHu, JHausinger, RPKarabencheva-Christova, TGChristov, CZInvited for the cover of this issue are Christo Z. Christov and co-workers at Michigan Technological University, University of Oxford, and Michigan State University. The image depicts the oxygen diffusion channel in class 7 histone demethylase (PHF8) and ethylene-forming enzyme (EFE) and changes in the enzymes’ conformations upon binding. Read the full text of the article at 10.1002/chem.202300138.
spellingShingle Chaturvedi, SS
Thomas, MG
Bathir Jaber Sathik Rifayee, S
White, W
Wildey, J
Warner, C
Schofield, CJ
Hu, J
Hausinger, RP
Karabencheva-Christova, TG
Christov, CZ
Dioxygen binding is controlled by the protein environment in non-heme FeII and 2-oxoglutarate oxygenases: a study on histone demethylase PHF8 and an ethylene-forming enzyme
title Dioxygen binding is controlled by the protein environment in non-heme FeII and 2-oxoglutarate oxygenases: a study on histone demethylase PHF8 and an ethylene-forming enzyme
title_full Dioxygen binding is controlled by the protein environment in non-heme FeII and 2-oxoglutarate oxygenases: a study on histone demethylase PHF8 and an ethylene-forming enzyme
title_fullStr Dioxygen binding is controlled by the protein environment in non-heme FeII and 2-oxoglutarate oxygenases: a study on histone demethylase PHF8 and an ethylene-forming enzyme
title_full_unstemmed Dioxygen binding is controlled by the protein environment in non-heme FeII and 2-oxoglutarate oxygenases: a study on histone demethylase PHF8 and an ethylene-forming enzyme
title_short Dioxygen binding is controlled by the protein environment in non-heme FeII and 2-oxoglutarate oxygenases: a study on histone demethylase PHF8 and an ethylene-forming enzyme
title_sort dioxygen binding is controlled by the protein environment in non heme feii and 2 oxoglutarate oxygenases a study on histone demethylase phf8 and an ethylene forming enzyme
work_keys_str_mv AT chaturvediss dioxygenbindingiscontrolledbytheproteinenvironmentinnonhemefeiiand2oxoglutarateoxygenasesastudyonhistonedemethylasephf8andanethyleneformingenzyme
AT thomasmg dioxygenbindingiscontrolledbytheproteinenvironmentinnonhemefeiiand2oxoglutarateoxygenasesastudyonhistonedemethylasephf8andanethyleneformingenzyme
AT bathirjabersathikrifayees dioxygenbindingiscontrolledbytheproteinenvironmentinnonhemefeiiand2oxoglutarateoxygenasesastudyonhistonedemethylasephf8andanethyleneformingenzyme
AT whitew dioxygenbindingiscontrolledbytheproteinenvironmentinnonhemefeiiand2oxoglutarateoxygenasesastudyonhistonedemethylasephf8andanethyleneformingenzyme
AT wildeyj dioxygenbindingiscontrolledbytheproteinenvironmentinnonhemefeiiand2oxoglutarateoxygenasesastudyonhistonedemethylasephf8andanethyleneformingenzyme
AT warnerc dioxygenbindingiscontrolledbytheproteinenvironmentinnonhemefeiiand2oxoglutarateoxygenasesastudyonhistonedemethylasephf8andanethyleneformingenzyme
AT schofieldcj dioxygenbindingiscontrolledbytheproteinenvironmentinnonhemefeiiand2oxoglutarateoxygenasesastudyonhistonedemethylasephf8andanethyleneformingenzyme
AT huj dioxygenbindingiscontrolledbytheproteinenvironmentinnonhemefeiiand2oxoglutarateoxygenasesastudyonhistonedemethylasephf8andanethyleneformingenzyme
AT hausingerrp dioxygenbindingiscontrolledbytheproteinenvironmentinnonhemefeiiand2oxoglutarateoxygenasesastudyonhistonedemethylasephf8andanethyleneformingenzyme
AT karabenchevachristovatg dioxygenbindingiscontrolledbytheproteinenvironmentinnonhemefeiiand2oxoglutarateoxygenasesastudyonhistonedemethylasephf8andanethyleneformingenzyme
AT christovcz dioxygenbindingiscontrolledbytheproteinenvironmentinnonhemefeiiand2oxoglutarateoxygenasesastudyonhistonedemethylasephf8andanethyleneformingenzyme