Heme & Hemoglobin as Biological Echoes of Prebiotic Redox Regulation: An Evolutionary Continuity from the Proto-Liver Origin of Life (PLOL)

This manuscript proposes that heme and hemoglobin are evolutionary descendants of the prebiotic redox-regulating systems described in the Proto-Liver Origin of Life (PLOL) framework.
Heme’s iron-porphyrin structure mirrors ancient mineral redox centers, and its chemistry reflects the same directional electron flow mechanisms proposed to stabilize early metabolism-like reactions. When embedded in a chiral protein pocket, heme acquires cooperative and regulatory properties, enabling hemoglobin to function as a distributed oxygen-control system across multicellular organisms.
This paper argues that hemoglobin retains structural and functional signatures of Earth’s earliest energy-stabilizing chemistry, creating a continuous lineage from prebiotic regulation → porphyrins → heme → hemoglobin → modern metabolic and physiological control (LBC framework).
The hypothesis yields testable predictions regarding porphyrin self-assembly, heme redox behavior, chirality-dependent binding dynamics, and ancestral hemoproteins.

Companion Paper B01 - Iron–Sulfur Clusters as Evolutionary Bridges in the Proto-Liver Origin of Life (PLOL) V1 added 17 Nov 2025

Keywords: heme evolution; hemoglobin; porphyrins; PLOL; redox regulation; prebiotic chemistry; oxygen transport; metabolic evolution; chirality; iron-sulfur chemistry.