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Computational and experimental insights into the mechanism of substrate recognition and feedback inhibition of protoporphyrinogen oxidase.

Hao GF1, Tan Y, Yang SG, Wang ZF, Zhan CG, Xi Z, Yang GF.
PloS one.PLoS One.2013 Jul 23;8(7):e69198. doi: 10.1371/journal.pone.0069198. Print 2013.
Protoporphyrinogen IX oxidase (PPO; EC 1.3.3.4) is an essential enzyme catalyzing the last common step in the pathway leading to heme and chlorophyll biosynthesis. Great interest in PPO inhibitors arises from both its significance to agriculture and medicine. However, the discovery of PPO inhibitors
PMID 23935953

Salmi M1, Tuomi J, Sirkkanen R, Ingman T, Mäkitie A.
The open dentistry journal.Open Dent J.2012;6:85-9. doi: 10.2174/1874210601206010085. Epub 2012 May 9.
Traditionally oral appliances i.e. removable orthodontic appliances, bite splints and snoring / sleep apnea appliances are made with alginate impressions and wax registrations. Our aim was to describe the process of manufacturing customized oral appliances with a new technique i.e. rapid tooling met
PMID 22615719

Functional definition of the tobacco protoporphyrinogen IX oxidase substrate-binding site.

Heinemann IU1, Diekmann N, Masoumi A, Koch M, Messerschmidt A, Jahn M, Jahn D.
The Biochemical journal.Biochem J.2007 Mar 15;402(3):575-80.
PPO (protoporphyrinogen IX oxidase) catalyses the flavin-dependent six-electron oxidation of protogen (protoporphyrinogen IX) to form proto (protoporphyrin IX), a crucial step in haem and chlorophyll biosynthesis. The apparent K(m) value for wild-type tobacco PPO2 (mitochondrial PPO) was 1.17 muM, w
PMID 17134376