https://www.ncbi.nlm.nih.gov/Structure/pdb/3IQF
3IQF: Structure of F420 dependent methylene-tetrahydromethanopterin dehydrogenase in complex with...
F420-dependent methylenetetrahydromethanopterin...
structuref420dependent
https://www.frontiersin.org/journals/microbiology/articles/10.3389/fmicb.2017.01902/full
Frontiers | Cofactor Tail Length Modulates Catalysis of Bacterial F420-Dependent Oxidoreductases
F420 is a microbial cofactor that mediates a wide range of physiologically important and industrially relevant redox reactions, including in methanogenesis a...
frontierscofactortaillength
https://elifesciences.org/articles/01963/peer-reviews
Peer review in Atomic model of the F420-reducing [NiFe] hydrogenase by electron cryo-microscopy...
The structure of a large enzyme complex involved in methanogenesis was determined at high resolution by electron cryo-microscopy.
https://www.ncbi.nlm.nih.gov/Structure/pdb/5JV4
5JV4: Structure of F420 binding protein, MSMEG_6526, from Mycobacterium smegmatis with F420 bound
Pyridoxamine 5'-phosphate oxidase-like FMN-binding protein(4S)-2-METHYL-2,4-PENTANEDIOLCOENZYME F420SODIUM ION
https://www.semanticscholar.org/topic/down-regulation-of-coenzyme-F420-dependent-activity/10770163
down regulation of coenzyme F420-dependent nitroreductase activity | Semantic Scholar
down regulationcoenzyme f420dependentnitroreductaseactivity
https://elifesciences.org/articles/01963
Atomic model of the F420-reducing [NiFe] hydrogenase by electron cryo-microscopy using a direct...
The structure of a large enzyme complex involved in methanogenesis was determined at high resolution by electron cryo-microscopy.